Render Target: STATIC
Render Timestamp: 2024-11-14T10:01:14.419Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-30 01:53:21.451
Product last modified at: 2024-11-07T22:15:11.437Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

BNIP3L/Nix (D4R4B) Rabbit mAb #12396

Filter:
  • WB
  • IP
  • IF

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 38, 76
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Immunofluorescence (Immunocytochemistry) 1:100 - 1:400

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    BNIP3L/Nix (D4R4B) Rabbit mAb recognizes endogenous levels of total BNIP3L/Nix protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu128 of human BNIP3L/Nix protein.

    Background

    BCL2/Adenovirus E1B 19 kDa protein-interacting protein 3-like (BNIP3L) (1), also termed BNIP3α (2), B5 (3), and Nix (4), is a member of the Bcl-2 family of apoptotic regulators with highest homology to BNIP3. BNIP3L can bind BNIP3, Bcl-xL, and Bcl-2 (1-5). BNIP3L forms homodimers that withstand denaturing by SDS and reducing conditions (5). BNIP3L is a mitochondrial protein and knockout studies suggest that BNIP3L regulates autophagic clearance of damaged mitochondria during erythroid maturation via mitochondrial autophagy (6,7). It has been shown that the expression of BNIP3L is up-regulated during terminal erythroid differentiation (6-8), as well as in tumor cell lines during hypoxia (9-11). BNIP3L directly regulates the elimination of mitochondria through its ability to bind to and recruit important components of the autophagic machinery, including LC3/Atg8 and GABARAP proteins, via its amino-terminal LC3-interacting region (LIR) (12). BNIP3L may also indirectly activate phagophore formation either via the recruitment of autophagy proteins or by binding Bcl-xL, which in turn releases Beclin-1 (13). BNIP3L/Nix also plays a pivotal role in Parkin-mediated mitochondrial autophagy via its ability to mediate the mitochondrial translocation of Parkin (14). Activated BNIP3L can promote the opening of mitochondrial permeability transition pores resulting in mitochondrial depolarization, generation of reactive oxygen species, and induction of necrosis. Due to its involvement in cell death and autophagy, research scientists have implicated BNIP3L in heart disease and cancer (13).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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