BAG Family Molecular Chaperone Regulator 2 (BAG2) is a member of the Bag family whose members compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. BAG2 contains 1 BAG domain and is a important component of the HSC 70/CHIP chaperone-dependent ubiquitin ligase complex. In mammalian cells BAG1, BAG2, and BAG3 bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.

BAG3 Protein, Mouse, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 77.7 kDa and the accession number is Q9JLV1.

BAG3 Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 63.7 kDa and the accession number is Q9JLV1.

Bcl-2-like protein 2 (BCL2L2) belongs to the Bcl-2 family. BCL2L2 is highly expressed in thebrain, spinal cord, testis, pancreas, heart, spleen, and mammary glands. BCL2L2 is a peripheral membrane protein containing three motifs, BH1, BH2 and BH4. The BH4 motif appears to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. BCL2L2 promotes cell survival and blocks dexamethasone-induced apoptosis. Furthermore, BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.

Cytochrome C (CYCS) is a small heme protein that belongs to the cytochrome c family. It is found loosely associated with the inner membrane of the mitochondrion. Cytochrome C is a highly soluble protein that functions as a central component of the electron transport chain in mitochondria. CYCS transfers electrons between Complexes III (Coenzyme Q - Cyt C reductase) and IV (Cyt C oxidase). CYCS 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 cytochrome c into the cytosol. Binding of Cytochrome C to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.

Caspase 14 is a member of the caspase family. Caspases are a kind of cysteine proteinase consisting of a prodomain plus large and small catalytic subunits, that play a central role in cell apoptosis. Caspase 14 possesses an unusually short prodomain and is highly expressed in embryonic tissues but absent from most of the adult tissues except for the skin, which suggests a role in ontogenesis and skin physiology. Unlike the other short prodomain caspases(caspase-3, caspase-6, and caspase-7), Caspase 14 was not processed by multiple death stimuli including activation of members of the tumor necrosis factor receptor family and expression of proapaptotic members of the bcl-2 family. Caspase 14 has been described to be processed and activated by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may take part in keratinocyte terminal differentiation, which is essential for the skin barrier.

BCL2L11, also known as Bim, belongs to the BCL-2 protein family. Members of this family form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. BCL2L11 contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and to act as an apoptotic activator. BCL2L11 gene functions as an essential initiator of apoptosis in thymocyte-negative selection.

Mouse interleukin-7(IL-7) is the member of hemopoietin family which is important to the differentiation, proliferation, and survival of lymphocyte. Mouse IL-7 shares approximately 88% aa sequence identity with rat IL-7 and 58-60% with human, equine, bovine, ovine, porcine, feline and canine IL-7. It is widely expressed in primary and secondary lymphoid tissues cell and stromal epithelial cells of the thymus, bone marrow, and intestines. IL-7 activation of IL-7 R alpha is critical for both T cell and B cell lineage development. It is important for proliferation during certain stages of B-cell maturation. IL-7 contributes to the maintenance of all naïve and memory T cells, mainly by promoting expression of the anti-apoptotic protein Bcl-2. It is required for optimal T cell-dendritic cell interaction.

B-cell lymphoma 2-related protein A1 (BCL2A1) is a member of the BCL-2 family of anti-apoptotic proteins that confers resistance to treatment with anti-cancer drugs. Immunohistochemical expression of Wnt11 and BCL2A1 in complete moles and normal villi. Bcl2 family proteins control mitochondrial apoptosis and its members exert critical cell type and differentiation stage-specific functions, acting as barriers against autoimmunity or transformation. Anti-apoptotic Bcl2a1/Bfl1/A1 is frequently deregulated in different types of blood cancers in humans but its physiological role is poorly understood as quadruplication of the Bcl2a1 gene locus in mice hampers conventional gene targeting strategies. In a physiological context, BCL2A1 is mainly expressed in the hematopoietic system, where it facilitates survival of selected leukocytes subsets and inflammation. However, BCL2A1 is overexpressed in a variety of cancer cells, including hematological malignancies and solid tumors, and may contribute to tumor progression. The development of small molecule inhibitors of BCL2A1 may be a promising approach mainly to sensitize tumor cells for apoptosis and thus improve the efficiency of anti-cancer therapy.

Bid, BH3-interacting domain death agonist, was initially cloned based in its ability to interact with both Bcl-2 and Bax. Bid contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. Bid is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. Bid is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals.

Death-associated protein kinase 1, also known as DAP kinase 1, DAPK1 and DAPK, is a cytoplasm protein which belongs to theprotein kinase superfamily, CAMK Ser / Thr protein kinase family and DAP kinase subfamily. DAPK1 contains tenANK repeats, onedeath domain and oneprotein kinase domain. DAPK1 is a calcium / calmodulin-dependent serine/threonine kinase which acts as a positive regulator of apoptosis. DAPK1 gene is a candidate tumor suppressor (TSG) and the abnormal methylation of DAPK1 gene has been found in many carcinomas. DAPK1 over-expression can induce cell apoptosis and inhibit tumor cell metastasis. DAPK1 gene over-expression could suppress PGCl3 cells malignant phenotype, inhibit PGCl3 cells growth, invasive, migration and adhesion ability, upregulate p53 gene and downregulate bcl-2 gene. Loss of activity of death-associated protein kinase 1 ( DAPK1 ) may be an independent factor affecting survival of non-small cell lung cancer patients. DAPK1 promoter methylation might play a significant role in the progression of chronic myeloid leukemia ( CML ).

BCL2 (B-cell leukemia/lymphoma 2, N-Histidine-tagged), also known as Bcl-2, belongs to the Bcl-2 family. Bcl-2 family proteins regulate and contribute to programmed cell death or apoptosis. It is a large protein family and all members contain at least one of four BH (bcl-2 homology) domains. Certain members such as Bcl-2, Bcl-xl and Mcl1 are anti-apoptotic, whilst others are pro-apoptotic. Most Bcl-2 family members contain a C-terminal transmembrane domain that functions to target these proteins to the outer mitochondrial and other intracellular membranes. It is expressed in a variety of tissues. BCL2 blocks the apoptotic death of some cells such as lymphocytes. It also regulates cell death by controlling the mitochondrial membrane permeability and inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor. 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. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy