Anti-BNIP3 Antibody Picoband® Fluoro647 Conjugated

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.

Apoptosis, Cancer, Cancer Metabolism, Cardiovascular, Cell Biology, Cell Death, Host-Virus Interaction, Interspecies Interaction, Intracellular, Metabolism, Metabolism Processes, Microbiology, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Pathways and Processes, Response To Hypoxia

Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. Plays an important role in the calprotectin (S100A8/A9) -induced cell death pathway.

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. 2. 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.

Mitochondrion. Mitochondrion outer membrane; Coexpression with the EIB 19- kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane.