|Reactivity||Human, Mouse, Rat|
|Product Name||Anti-BNIP3 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for BCL2/adenovirus E1B 19 kDa protein-interacting protein 3(BNIP3) detection. Tested with WB in Human;Mouse;Rat.|
|Cite This Product||Anti-BNIP3 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1057)|
|Immunogen||A synthetic peptide corresponding to a sequence at the N-terminus of human BNIP3(38-53aa IYNGDMEKILLDAQHE), identical to the related mouse and rat sequences.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
Images And Assay Conditions
Anti-BNIP3 antibody, PA1057, Western blotting
All lanes: Anti BNIP3 (PA1057) at 0.5ug/ml
Lane 1: HELA Whole Cell Lysate at 40ug
Lane 2: MM231Whole Cell Lysate at 40ug
Predicted bind size: 22KD
Observed bind size: 30KD
Protein Target Info (Source: Uniprot.org)
|Protein Name||BCL2/adenovirus E1B 19 kDa protein-interacting protein 3|
|Alternative Names||BCL2/adenovirus E1B 19 kDa protein-interacting protein 3;BNIP3;NIP3;|
|Subcellular Localization||Mitochondrion. Mitochondrion outer membrane; Single-pass membrane protein. 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.|
|Molecular Weight||21541 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||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 to 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. .|
|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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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,