Proteins & Peptides

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.

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.

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.

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.

BIRC3 or baculoviral IAP repeat containing 3 is a member of the IAP family of proteins. BIRC3 inhibit apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2 and thereby interfering with activation of ICE-like proteases. BIRC3 inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. BIRC3 is a potential oncogene which is overexpressed in multiple lung cancers with or without higher copy numbers (1). BIRC3 is a key regulator of NOD innate immunity signaling (2). BIRC3 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cell Cycle, and Inflammation research.

BIRC3 or baculoviral IAP repeat containing 3 is a member of the IAP family of proteins. BIRC3 inhibit apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2 and thereby interfering with activation of ICE-like proteases. BIRC3 inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. BIRC3 is a potential oncogene which is overexpressed in multiple lung cancers with or without higher copy numbers (1). BIRC3 is a key regulator of NOD innate immunity signaling (2). BIRC3 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cell Cycle, and Inflammation research.

BMP2K or Bone morphogenic protein 2 inducible kinase is the human homolog of mouse BMP-2-inducible kinase which plays a key role in skeletal development and patterning. BMP2K is a serine/threonine protein kinase which contains a nuclear localization signal and plays a regulatory role in attenuating the program of osteoblast differentiation. BMP2K gene is strongly correlated with high myopia and may contribute to a genetic risk factor for high degrees of myopic pathogenesis (1). BMP-2 expression is suppressed by an EP4 receptor antagonist and PGE2 produced by COX-2 increases BMP-2 expression via binding the EP4 receptor (2). BMP2K Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Cancer, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, JNK/SAPK Pathway, NfkB Pathway, p38 Pathway, PKA/PKC Pathway, and WNT Signaling research.