Rabbit Bax Polyclonal Antibody | anti-Bax antibody

Bax (A20) Antibody

Cat. Num. AAA440005

• Reactivity: Mouse, Rat, Human
• Applications: Western Blot, Immunoprecipitation, Immunohistochemistry
• Synonyms: Bax; Polyclonal Antibody; Bax (A20) Antibody; anti-Bax antibody

• Host: Rabbit
• Reactivity: Mouse, Rat, Human
• Clonality: Polyclonal
• Form/Format: 200 ug/ml rabbit polyclonal IgG in 1 ml PBS containing 0.1 % sodium azide and 0.2% gelatin.
• Sequence Length: 133

• Applicable Applications for anti-Bax antibody: Western Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC)
• Application Notes: Western Blot starting dilution: 1:400
• Origin: Bax is provided as an affinity purified rabbit polyclonal antibody, raised against a peptide mapping to the amino terminus of human Bax.
• Competition Studies: A blocking peptide is lso available, MBS443005, for use in competition studies. Each vial contains 100ug of peptide in 0.5ml PBS with 0.1% sodium azide and 100 ug BSA.
• Preparation and Storage: Store this product at 4 degree C, do not freeze. The product is stable for one year from the date of shipment.

Western Blot (WB)

Related Product Information for anti-Bax antibody

Bcl-2 family of proteins is a key regulator of apoptosis that function to either inhibit or promote cell death. The over expression of members such as Bcl-2 and Bcl-xL inhibit the apoptotic process (1,2). The Bcl-2 family members are also characterized by dimerizing to further modulate apoptosis. Bag-1, for example, has been found to form a heterodimer with Bcl-2 resulting in the enhancement of the anti-apoptotic effect of Bcl-2 (3,4). Other anti-apoptotic Bcl-2 family members include A1, Bcl-xg, Bcl-xb, Mcl-1, BAR, BI-1 and Bcl-w (5). The pro-apoptotic family members include Bax, Bcl-xS, Bad, Bak, NBK, BID, Hrk, Bok, Bim, Noxa and Diva. Bax and Bak have been shown to play a critical role in cytochrome c release from mitochondria and thus initiate apoptosis (6). Bad plays a critical role in the Bax-mediated apoptosis pathway by dimerizing with Bcl-xL, causing the displacment of Bax. The displacement of Bax allows apoptosis to proceed (7). Bcl-xS, a shorter version of Bcl-xL (lacking amino acids 126-188), apparently utilizes a different pathway than Bax to induce cell death. Some research suggests that Bcl-xS uses a novel mechanism for regulating caspase or it may use an alternate cell death effector pathway (8,9).

References

1.) You WK, Seo HJ, Chung KH, Kim DS. 2003. A novel metalloprotease from Gloydius halys venom induces endothelial cell apoptosis through its protease and disintegrin-like domains. J Biochem (Tokyo) Nov;134(5):739-49. 2.) Kim J, Seong J, and Kim SH. 2004. Enhancement of Tumor Response by Farnesyltransferase Inhibitor in C3H/HeJ Hepatocarcinoma. Ann N Y Acad Sci. Dec;1030:95-102. 3.) Ma D, Hossain M, Chow A, Arshad M, Battson RM, Sanders RD, Mehmet H, Edwards AD, Franks NP, Maze M. 2005. Xenon and hypothermia combine to provide neuroprotection from neonatal asphyxia. Ann Neurol. Aug;58(2):182-93.4.) Wan Y, Xu J, Ma D, Zeng Y, Cibelli M, Maze M. 2007. Postoperative impairment of cognitive function in rats: a possible role for cytokine-mediated inflammation in the hippocampus. Anesthesiology. Mar;106(3):436-43.

1. Huang Z. 2000. Bcl-2 family proteins as targets for anticancer drug design. Oncogene 19(56): 6627-66312. Reed JC. 1997. Double identity for proteins of the Bcl-2 family. Nature 387(6635): 773-7763. Eversole-Cire P, Concepcion FA, Simon MI, Takayama S, Reed JC, Chen J. 2000. Synergistic effect of Bcl-2 and BAG-1 on the prevention of photoreceptor cell death. Invest Ophthalmol Vis Sci 41(7): 1953-19614. Coldwell MJ, deSchoolmeester ML, Fraser GA, Pickering BM, Packham G, Willis AE. 2001. The p36 isoform of BAG-1 is translated by internal ribosome entry following heat shock. Oncogene 20(30): 4095-41005. Bae j, Hsu SY, Leo CP, Zell K, Hsueh AJ. 2001. Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis. Apoptosis 6(5): 319-3306. Wei MC, Zong WX, Cheng EH, Lindsten T, Panoutsakopoulou V, Ross AJ, Roth KA, MacGregor GR, Thompson CB, Korsmeyer SJ. 2001. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292(5517): 624-6267. Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ. 1995. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80(2): 285-2918. Fridman JS, Parsels J, Rehemtulla A, Maybaum J. 2001. Cytochrome c depletion upon expression of Bcl-XS. J Biol Chem 276(6): 4205-109. Lindenboim L, Yuan J, Stein R. 2000. Bcl-xS and Bax induce different apoptotic pathways in PC12 cells. Oncogene 19(14): 1783-1793

NCBI and Uniprot Product Information

• NCBI GI #: 975870
• NCBI GeneID: 24887
• UniProt Accession #: Q63690; Q62995; Q64383
• NCBI Official Full Name: bax, partial
• NCBI Official Synonym Full Names: Bcl2-associated X protein
• NCBI Official Symbol: Bax
• NCBI Protein Information: apoptosis regulator BAX
• UniProt Protein Name: Apoptosis regulator BAX
• Protein Family: Bax inhibitor
• UniProt Gene Name: Bax
• UniProt Entry Name: BAX_RAT

NCBI Description

Bcl2-related gene; involved in the regulation of apoptotic cell death [RGD, Feb 2006]

Uniprot Description

BAX: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. Homodimer. Forms higher oligomers under stress conditions. Interacts with BCL2L11. Interaction with BCL2L11 promotes BAX oligomerization and association with mitochondrial membranes, with subsequent release of cytochrome c. Forms heterodimers with BCL2, E1B 19K protein, BCL2L1 isoform Bcl-X(L), BCL2L2, MCL1 and A1. Interacts with SH3GLB1 and HN. Interacts with SFN and YWHAZ; the interaction occurs in the cytoplasm. Under stress conditions, JNK-mediated phosphorylation of SFN and YWHAZ, releases BAX to mitochondria. Isoform Sigma interacts with BCL2A1 and BCL2L1 isoform Bcl-X(L). Interacts with RNF144B, which regulates the ubiquitin-dependent stability of BAX. Interacts with CLU under stress conditions that cause a conformation change leading to BAX oligomerization and association with mitochondria. Does not interact with CLU in unstressed cells. Interacts with FAIM2/LFG2. Interacts with human cytomegalovirus/HHV-5 protein vMIA/UL37. Expressed in a wide variety of tissues. Isoform Psi is found in glial tumors. Isoform Alpha is expressed in spleen, breast, ovary, testis, colon and brain, and at low levels in skin and lung. Isoform Sigma is expressed in spleen, breast, ovary, testis, lung, colon, brain and at low levels in skin. Isoform Alpha and isoform Sigma are expressed in pro- myelocytic leukemia, histiocytic lymphoma, Burkitt's lymphoma, T- cell lymphoma, lymphoblastic leukemia, breast adenocarcinoma, ovary adenocarcinoma, prostate carcinoma, prostate adenocarcinoma, lung carcinoma, epidermoid carcinoma, small cell lung carcinoma and colon adenocarcinoma cell lines. Belongs to the Bcl-2 family. 8 isoforms of the human protein are produced by alternative splicing.

Protein type: Apoptosis; Tumor suppressor; Membrane protein, integral; Mitochondrial

Cellular Component: mitochondrial permeability transition pore complex; endoplasmic reticulum membrane; mitochondrion; cell; endoplasmic reticulum; nuclear envelope; cytosol; pore complex; mitochondrial outer membrane; membrane; mitochondrial membrane; cytoplasm; intracellular; nucleus

Molecular Function: BH domain binding; identical protein binding; protein binding; protein homodimerization activity; protein heterodimerization activity; channel activity; chaperone binding; heat shock protein binding; protein complex binding; BH3 domain binding; lipid binding

Biological Process: hypothalamus development; regulation of cell cycle; positive regulation of apoptosis; response to toxin; myeloid cell homeostasis; germ cell programmed cell death; homeostasis of number of cells; B cell apoptosis; post-embryonic development; germ cell development; regulation of mammary gland epithelial cell proliferation; spermatid differentiation; development of secondary sexual characteristics; regulation of mitochondrial membrane potential; protein insertion into mitochondrial membrane during induction of apoptosis; regulation of neuron apoptosis; establishment and/or maintenance of transmembrane electrochemical gradient; negative regulation of neuron apoptosis; kidney development; negative regulation of protein binding; response to corticosterone stimulus; inner mitochondrial membrane organization and biogenesis; response to drug; nervous system development; release of cytochrome c from mitochondria; outer mitochondrial membrane organization and biogenesis; positive regulation of B cell apoptosis; regulation of protein homodimerization activity; cellular respiration; vagina development; protein oligomerization; fertilization; induction of apoptosis via death domain receptors; DNA damage response, signal transduction resulting in induction of apoptosis; negative regulation of fibroblast proliferation; retina development in camera-type eye; reduction of endoplasmic reticulum calcium ion concentration; glycosphingolipid metabolic process; response to ionizing radiation; mitochondrial fragmentation during apoptosis; cerebral cortex development; regulation of nitrogen utilization; post-embryonic camera-type eye morphogenesis; positive regulation of pigmentation; regulation of protein heterodimerization activity; T cell homeostatic proliferation; apoptosis; negative regulation of peptidyl-serine phosphorylation; neuron migration; positive regulation of apoptosis involved in mammary gland involution; regulation of caspase activity; response to salt stress; release of matrix enzymes from mitochondria; negative regulation of cell proliferation; positive regulation of protein oligomerization; apoptotic mitochondrial changes; B cell homeostatic proliferation; B cell homeostasis; ovarian follicle development; positive regulation of neuron apoptosis; response to wounding; response to gamma radiation; response to axon injury; B cell negative selection; protein homooligomerization; leukocyte homeostasis; caspase activation; transformed cell apoptosis; mitochondrial fusion; male gonad development; Sertoli cell proliferation; response to cocaine; limb morphogenesis; odontogenesis of dentine-containing teeth; cell proliferation; neuron apoptosis; response to copper ion; homeostasis of number of cells within a tissue; spermatogenesis; retinal cell programmed cell death; blood vessel remodeling; positive regulation of release of sequestered calcium ion into cytosol; brain development; caspase activation via cytochrome c; response to DNA damage stimulus; sex differentiation