Proteins & Peptides

ATG13 is a protein that is part of the autophagy complex which is the major route by which cytoplasmic contents are delivered to the lysosome for degradation. ATG13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. In mammals, ATG13 interacts with ATG1 (ULK1/2) and FIP200 to form the autophagy. ATG101 can also bind to ATG13 protein and is important for the stability and basal phosphorylation of ATG13 and ULK1 (1). mTOR can suppress the autophagy process through direct regulation of the ULK1-Atg13-FIP200 complex where mTOR has been shown to phosphorylate ATG13 (2). ATG13 Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, Angiogenesis, Angiogenesis, Apoptosis/Autophagy, Apoptosis/Autophagy, Cardiovascular Disease, Cardiovascular Disease, Cellular Stress, Cellular Stress, Inflammation, Inflammation, Metabolic Disorder, Metabolic Disorder, Neurobiology, Neurobiology, NfkB Pathway, NfkB Pathway, p38 Pathway, and

BAD is a member of the BCL-2 family of proteins that are known to be regulators of programmed cell death. BAD is a pro-apoptotic protein that forms a heterodimer complex with BCL-xL and BCL-2 which reverses the prosurvival activity of these proteins (1). The proapoptotic activity of BAD is regulated through its phosphorylation and this inhibits the pro-apoptosis function of BAD. Protein kinases such as AKT, RAF and RSK1 can phosphorylate BAD and RSK1-induced phosphorylation of BAD at ser112 suppresses BAD-mediated apoptosis in neurons. BAD inhibits G(1) to S phase transition in MCF7 breast cancer cells and overexpression of BAD inhibits cell growth as well as cyclin D1 expression (2). BAD Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, Apoptosis/Autophagy, Cancer, Cellular Stress, and Neurobiology research.

BAD is a member of the BCL-2 family of proteins that are known to be regulators of programmed cell death. BAD is a pro-apoptotic protein that forms a heterodimer complex with BCL-xL and BCL-2 which reverses the prosurvival activity of these proteins (1). The proapoptotic activity of BAD is regulated through its phosphorylation and this inhibits the pro-apoptosis function of BAD. Protein kinases such as AKT, RAF and RSK1 can phosphorylate BAD and RSK1-induced phosphorylation of BAD at ser112 suppresses BAD-mediated apoptosis in neurons. BAD inhibits G(1) to S phase transition in MCF7 breast cancer cells and overexpression of BAD inhibits cell growth as well as cyclin D1 expression (2). BAD Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, Apoptosis/Autophagy, Cancer, Cellular Stress, and Neurobiology research.

BAG1 (also known as BCL2-associated athanogene) is a membrane protein rich in glutamic acid residues that binds to BCL2 and blocks apoptosis or programmed cell death (1). The BAG1-BCL2 complex enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms (2). Overexpression of BAG1 in 3T3 fibroblasts prevents apoptosis in the presence of low serum. BAG1 has also been shown to interact with activated glucocorticoid, androgen, estrogen and progesterone receptors. Binding to these receptors by BAG1 is dependent on receptor activation. BAG1 Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, and Neurobiology research.

BAG1 (also known as BCL2-associated athanogene) is a membrane protein rich in glutamic acid residues that binds to BCL2 and blocks apoptosis or programmed cell death (1). The BAG1-BCL2 complex enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms (2). Overexpression of BAG1 in 3T3 fibroblasts prevents apoptosis in the presence of low serum. BAG1 has also been shown to interact with activated glucocorticoid, androgen, estrogen and progesterone receptors. Binding to these receptors by BAG1 is dependent on receptor activation. BAG1 Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, and Neurobiology research.

BAX is a proapoptotic protein of the BCL2 protein family. BAX forms a heterodimer with BCL2 and functions as an apoptotic activator. BAX interacts with and increases the opening of the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in the mitochondrial membrane potential and the release of cytochrome c (1). The expression of BAX gene is regulated by the tumor suppressor p53 and BAX has been shown to be involved in p53-mediated apoptosis. Multiple alternatively spliced transcript variants, which encode different isoforms, have been reported for this gene (2). BAX Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, and Neurobiology research.

BAX is a proapoptotic protein of the BCL2 protein family. BAX forms a heterodimer with BCL2 and functions as an apoptotic activator. BAX interacts with and increases the opening of the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in the mitochondrial membrane potential and the release of cytochrome c (1). The expression of BAX gene is regulated by the tumor suppressor p53 and BAX has been shown to be involved in p53-mediated apoptosis. Multiple alternatively spliced transcript variants, which encode different isoforms, have been reported for this gene (2). BAX Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, and Neurobiology research.

BCKDK or branched chain alpha-keto acid dehydrogenase kinase is an important regulator of the valine, leucine, and isoleucine catabolic pathways. BCKDK is found in the mitochondrion where it phosphorylates and inactivates BCKD. The branched-chain alpha-keto dehydrogenase complex (BCKDH) catalyzes the rate-limiting step in the oxidation of branched-chain amino acids and BCKDK inactivates the BCKDH complex by catalyzing serine phosphorylation of the E1-alpha subunit (1). BCKDH kinase catalyzes the serine phosphorylation of the E1- alpha subunit of BCKDH (2). BCKDK Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, and Metabolic Disorder research.

BCKDK or branched chain alpha-keto acid dehydrogenase kinase is an important regulator of the valine, leucine, and isoleucine catabolic pathways. BCKDK is found in the mitochondrion where it phosphorylates and inactivates BCKD. The branched-chain alpha-keto dehydrogenase complex (BCKDH) catalyzes the rate-limiting step in the oxidation of branched-chain amino acids and BCKDK inactivates the BCKDH complex by catalyzing serine phosphorylation of the E1-alpha subunit (1). BCKDH kinase catalyzes the serine phosphorylation of the E1- alpha subunit of BCKDH (2). BCKDK Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, and Metabolic Disorder research.