Other Proteins

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.

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.

BCL2 gene encodes an integral inner mitochondrial membrane protein that acts as an antiapoptotic protein (1). The protein BAD can antagonize both the cell cycle and antiapoptotic functions of BCL2 through binding to the BH3 domain. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma (2). BCL2 is phosphorylated on specific serine/threonine residues within the unstructured loop in response to diverse stimuli and such phosphorylation has been associated with the loss of the biological function of BCL2. BCL2 Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, Apoptosis/Autophagy, Cancer, Cellular Stress, and Neurobiology research.

BCR (also known as breakpoint cluster region) encodes a phosphoprotein that has serine/threonine kinase activity (1). The human c-ABL oncogene is translocated from chromosome 9 to a region on chromosome 22 (associated with BCR) in chronic myelocytic leukemia. In classical t(9;22) translocation, as observed in chronic granulocytic leukemia (CGL), a hybrid DNA unit is produced comprising the BCR gene product plus the translocated c-ABL gene from chromosome 9. The BCR-ABL hybrid protein (p210) is formed that displays increased tyrosine kinase activity. A similar DNA rearrangement of the p210 protein is also found in cases of Philadelphia-positive acute lymphoblastic leukemia (ALL) (2). BCR Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, and Cancer research.

BID is a BH3 interacting death domain that heterodimerizes with either agonist BAX or antagonist BCL2 (1). BID is a member of the BCL-2 family of cell death regulators and is a mediator of mitochondrial damage induced by caspase-8 (CASP8). BID initiates apoptosis by binding to regulatory sites on prosurvival BCL2 proteins to directly neutralize their function. Multiple alternatively spliced transcript variants of BID have been found, but the full-length nature of some variants has not been defined. BID together with Cathepsins play an important role in the actions of Camptothecin on breast cancer cells (2). BID Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, and Neurobiology research.

BUB1 is a kinase which involved in spindle checkpoint function that in part by phosphorylating a member of the miotic checkpoint complex and activating the spindle checkpoint. BUB1 is highly expressed in thymus, ovary, and testis (1). BUB1 maintains the steady-state level and centromeric localization of SGO1, and they concluded that BUB1 protects centromeric cohesion in mitosis through SGO1 (2). BUB1-mediated phosphorylation of CDC20 is required for proper checkpoint signaling and that inhibition of APC by BUB1 may partly account for the sensitivity of the spindle checkpoint. BUB1 kinase creates a mark for shugoshin localization and the correct partitioning of chromosomes. BUB1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.

Calmodulin 1 is a member of calcium-modulated proteins which is present in the cytosol and on membranes facing the cytosol and has a high affinity for calcium. Calmodulin 1 has 4 calcium-binding domains and plays a role in cell growth, cell cycle, signal transduction and the synthesis and release of neurotransmitters. Calmodulin can bind to the epidermal growth factor receptor at its cytosolic juxtamembrane region and this inhibits its tyrosine kinase activity (1). A number of other proteins including HSP70 have been shown to interact with Calmodulin 1 in a cell-phase-specific manner (2). Calmodulin 1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, ERK/MAPK Pathway, Neurobiology, and PKA/PKC Pathway research.