

Supplier:
BOSTER IMMUNOLEADERCat no: PA1057
Polyclonal Anti-NIP3/BNIP3
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SPECIFICATIONS
Price
200.00 USD
Catalog Number
PA1057
Size
100ug/vial
Applications
WB
Reactivities
Hum, Mouse, Rat
Form
Lyophilized
Format
Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
Gene Id
BNIP3
References
1. Burton TR, Henson ES, Baijal P, Eisenstat DD, Gibson SB. The pro-cell death Bcl-2 family member, BNIP3, is localized to the nucleus of human glial cells: Implications for glioblastoma multiforme tumor cell survival under hypoxia. Int J Cancer. 2006 Apr 1; 118(7):1660-9.\n2. Ray R, Chen G, Vande Velde C, Cizeau J, Park JH, Reed JC, Gietz RD, Greenberg AH. BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites. J Biol Chem. 2000 Jan 14; 275(2):1439-48.
Swiss Prot
Q12983
Storage Temp
\"At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.\nAvoid repeated freezing and thawing. \n\"\n
Additional Info
A synthetic peptide corresponding to a sequence at the N-terminal of human NIP3, identical to the related mouse and rat sequences.
Scientific Background
The Bcl-2 nineteen kilodalton interacting protein 3 (BNIP3 or NIP3), is a hypoxia-inducible proapoptotic member of the Bcl-2 family that induces cell death by associating with the mitochondria. BNIP3, expressed in skeletal muscle and in the brain at low levels, is primarily localized to the nucleus of glial cells of the normal human brain, as well as in the malignant glioma cell line U251. BNIP3 expression in the cytoplasm increases and localizes with the mitochondria, contributing to induction of cell death. Cellular protein BNIP3 interacts with E1B-19K, BCL-2, BCL-xL, and EBV-BHRF1. BNIP3 contains Bcl-2 homology 3 (BH3) domain and COOH-terminal transmembrane (TM) domain. The BH3 domain of BNIP3 mediates Bcl-2/Bcl-X(L) heterodimerization and confers pro-apoptotic activity; whereas the TM domain is critical for homodimerization, pro-apoptotic function, and mitochondrial targeting.
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