Biology hyperlinks temporal protein adjustments to drug responses in a melanoma cell
FloraSeptember 15, 20200 Comments
CCR2 of Tumor Microenvironmental Cells Is a Related Modulator of Glioma Biology
Glioblastoma multiforme (GBM) reveals a excessive inflow of tumor-associated macrophages (TAMs). The CCR2/CCL2 pathway is taken into account a related sign for the recruitment of TAMs and has been urged as a therapeutic goal in malignant gliomas. We discovered that TAMs of human GBM specimens and of a syngeneic glioma mannequin specific CCR2 to various extents.
Utilizing a Ccr2-deficient pressure for glioma inoculation revealed a 30% discount of TAMs intratumorally. This diminished immune cell infiltration occurred with augmented tumor volumes probably based mostly on elevated cell proliferation. Remaining TAMs in Ccr2-/- mice confirmed comparable floor marker expression patterns compared to wildtype mice, however expression ranges of inflammatory transcription components (Stat3, Irf7, Cox2) and cytokines (Ifnβ, Il1β, Il12α) had been significantly affected.
Moreover, we demonstrated an impression on blood vessel integrity, whereas vascularization of tumors appeared related between mouse strains. The upper stability and attenuated leakiness of the tumor vasculature indicate improved sustenance of glioma tissue in Ccr2-/- mice. Moreover, regardless of TAMs residing within the perivascular area of interest in Ccr2-/- mice, their pro-angiogenic exercise was decreased by the downregulation of Vegf. In conclusion, missing CCR2 solely on tumor microenvironmental cells results in enhanced tumor development, whereby excessive numbers of TAMs infiltrate gliomas independently of the CCR2/CCL2 sign.
Perturbation biology hyperlinks temporal protein adjustments to drug responses in a melanoma cell line
Most cancers cells have genetic alterations that always immediately have an effect on intracellular protein signaling processes permitting them to bypass management mechanisms for cell dying, development and division. Most cancers medication focusing on these alterations usually work initially, however resistance is widespread. Combos of focused medication could overcome or forestall resistance, however their choice requires context-specific information of signaling pathways together with complicated interactions resembling suggestions loops and crosstalk.
To deduce quantitative pathway fashions, we collected a wealthy dataset on a melanoma cell line: Following perturbation with 54 drug combos, we measured 124 (phospho-)protein ranges and phenotypic response (cell development, apoptosis) in a time sequence from 10 minutes to 67 hours.
From these knowledge, we educated time-resolved mathematical fashions that seize molecular interactions and the coupling of molecular ranges to mobile phenotype, which in flip reveal the primary direct or oblique molecular responses to every drug. Systematic mannequin simulations recognized novel combos of medication predicted to cut back the survival of melanoma cells, with partial experimental verification. This specific software of perturbation biology demonstrates the potential impression of mixing time-resolved knowledge with modeling for the invention of recent combos of most cancers medication.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Adrenergic Receptor Beta 1 (ADRb1) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Adrenergic Receptor Beta 1 (ADRb1) in tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Adrenergic Receptor Beta 1 (ADRb1) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: Quantitative sandwich ELISA for measuring Rat Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Rat Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Rat Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Rat Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Rat Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Quantitativesandwich ELISA kit for measuring Human Beta-1 adrenergic receptor (ADRB1) in samples from serum, plasma, tissue homogenates, cell lysates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitativesandwich ELISA kit for measuring Human Beta-1 adrenergic receptor(ADRB1) in samples from serum, plasma, tissue homogenates, cell lysates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
Human Beta-1 Adrenergic Receptor (ADRB1) ELISA Kit
Description: A sandwich quantitative ELISA assay kit for detection of Human Adrenergic Receptor Beta 1 (ADRb1) in samples from serum, plasma, tissue homogenates or other biological fluids.
Human Adrenergic Receptor Beta 1 (ADRb1) ELISA Kit
Description: A sandwich quantitative ELISA assay kit for detection of Human Adrenergic Receptor Beta 1 (ADRb1) in samples from serum, plasma, tissue homogenates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Adrenergic Receptor Beta 1 (ADRb1) in samples from tissue homogenates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Adrenergic Receptor Beta 1 (ADRb1) in samples from tissue homogenates or other biological fluids.
Human Adrenergic Receptor Beta 1 (ADRb1) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates, cell lysates and other biological fluids.
Human Adrenergic Receptor Beta 1 (ADRb1) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates, cell lysates and other biological fluids.
Human Adrenergic Receptor Beta 1 (ADRb1) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates, cell lysates and other biological fluids.
Human Adrenergic Receptor Beta 1 (ADRb1) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates, cell lysates and other biological fluids.
Human Adrenergic Receptor Beta 1 (ADRb1) ELISA Kit
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Adrenergic Receptor Beta 1 (ADRb1) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Adrenergic Receptor Beta 1 (ADRb1) in Tissue homogenates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Adrenergic Receptor Beta 1 (ADRb1) in samples from Tissue homogenates and other biological fluids. with no significant corss-reactivity with analogues from other species.
Human Adrenergic Receptor Beta 1 (ADRb1) ELISA Kit
Description: A sandwich ELISA kit for detection of Adrenergic Receptor Beta 1 from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Pig Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Pig Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Pig Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Pig Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Pig Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Mouse Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Mouse Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Mouse Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Mouse Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Mouse Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Human Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Human Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Human Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Human Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Human Beta-1 adrenergic receptor (ADRB1)
Description: Quantitative sandwich ELISA for measuring Human Beta-1 adrenergic receptor (ADRB1) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: A sandwich ELISA kit for detection of Adrenergic Receptor Beta 1 from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
ELISA kit for Human ADRb1 (Adrenergic Receptor Beta 1)
Description: A sandwich ELISA kit for detection of Adrenergic Receptor Beta 1 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
Description: A competitive ELISA for quantitative measurement of Rat β 1 adrenergic receptor(ADRB1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
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On the leading edge: protease-based strategies for sensing and controlling cellbiology
Sequence-specific proteases have confirmed to be versatile constructing blocks for instruments that report or management mobile perform. Reporting strategies hyperlink protease exercise to biochemical alerts, whereas management strategies depend on engineering proteases to reply to exogenous inputs resembling gentle or chemical substances.
In flip, proteases have inherent management skills, as their native features are to launch, activate or destroy proteins by cleavage, with the irreversibility of proteolysis permitting sustained downstream results. In consequence, protease-based artificial circuits have been created for various makes use of resembling reporting mobile signaling, tuning protein expression, controlling viral replication and detecting most cancers states. Right here, we comprehensively evaluate the event and software of protease-based strategies for reporting and controlling mobile perform in eukaryotes.
Description: CYCS is also known as CYC, HCS or THC4. This gene encodes a small heme protein that functions as a central component of the electron transport chain in mitochondria. The encoded protein associates with the inner membrane of the mitochondrion where it accepts electrons from cytochrome b and transfers them to the cytochrome oxidase complex. This protein is also involved in initiation of apoptosis. Mutations in this gene are associated with autosomal dominant nonsyndromic thrombocytopenia. Numerous processed pseudogenes of this gene are found throughout the human genome.
Description: CYCS is also known as CYC, HCS or THC4. This gene encodes a small heme protein that functions as a central component of the electron transport chain in mitochondria. The encoded protein associates with the inner membrane of the mitochondrion where it accepts electrons from cytochrome b and transfers them to the cytochrome oxidase complex. This protein is also involved in initiation of apoptosis. Mutations in this gene are associated with autosomal dominant nonsyndromic thrombocytopenia. Numerous processed pseudogenes of this gene are found throughout the human genome.
Description: CYCS is also known as CYC, HCS or THC4. This gene encodes a small heme protein that functions as a central component of the electron transport chain in mitochondria. The encoded protein associates with the inner membrane of the mitochondrion where it accepts electrons from cytochrome b and transfers them to the cytochrome oxidase complex. This protein is also involved in initiation of apoptosis. Mutations in this gene are associated with autosomal dominant nonsyndromic thrombocytopenia. Numerous processed pseudogenes of this gene are found throughout the human genome.
Description: Cytochrome c is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
Description: Cytochrome c is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
Description: Cytochrome c is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
Description: It recognizes an epitope within amino acids 93-104 of pigeon Cytochrome C, a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: It recognizes an epitope within amino acids 93-104 of pigeon Cytochrome C, a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: It recognizes an epitope within amino acids 93-104 of pigeon Cytochrome C, a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: It recognizes an epitope within amino acids 93-104 of pigeon Cytochrome C, a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
Description: Cytochrome C, or CYCS, is an electron carrier protein. The oxidized form of the CYCS heme group can accept an electron from the heme group of the Cytochrome C1 subunit of cytochrome reductase. CYCS then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; CYCS also plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of CYCS into the cytosol. Binding to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. [UniProt]
Description: Cytochrome C, or CYCS, is an electron carrier protein. The oxidized form of the CYCS heme group can accept an electron from the heme group of the Cytochrome C1 subunit of cytochrome reductase. CYCS then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; CYCS also plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of CYCS into the cytosol. Binding to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. [UniProt]
Description: Cytochrome C, or CYCS, is an electron carrier protein. The oxidized form of the CYCS heme group can accept an electron from the heme group of the Cytochrome C1 subunit of cytochrome reductase. CYCS then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; CYCS also plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of CYCS into the cytosol. Binding to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. [UniProt]
Description: Cytochrome C, or CYCS, is an electron carrier protein. The oxidized form of the CYCS heme group can accept an electron from the heme group of the Cytochrome C1 subunit of cytochrome reductase. CYCS then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; CYCS also plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of CYCS into the cytosol. Binding to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. [UniProt]
Description: In mammalian cells, the highly conserved cytochrome C protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e. cytochrome in the mitochondria with heme attached).
Description: In mammalian cells, the highly conserved cytochrome C protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e. cytochrome in the mitochondria with heme attached).
Description: In mammalian cells, the highly conserved cytochrome C protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e. cytochrome in the mitochondria with heme attached).
Description: In mammalian cells, the highly conserved cytochrome C protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e. cytochrome in the mitochondria with heme attached).
Description: In mammalian cells, the highly conserved cytochrome C protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e. cytochrome in the mitochondria with heme attached).
Description: In mammalian cells, the highly conserved cytochrome C protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e. cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This mAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human Cytochrome c . This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human Cytochrome c . This antibody is tested and proven to work in the following applications:
