Product Pathways - Autophagy Signaling
BNIP3L/Nix (D4R4B) Rabbit mAb #12396
|W IP IF-IC||H M R Mk||Endogenous||38, 76||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
BNIP3L/Nix (D4R4B) Rabbit mAb recognizes endogenous levels of total BNIP3L/Nix protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu128 of human BNIP3L/Nix protein.
Western blot analysis of A172 and HeLa cells, untreated (-) or cobalt chloride-treated (100 μM, overnight; +), using BNIP3L/Nix (D4R4B) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower).
Western blot analysis of extracts from various cell lines using BNIP3L/Nix (D4R4B) Rabbit mAb.
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing DYKDDDDK-tagged full-length human BNIP3L/Nix (hBNIP3L/Nix-DYKDDDDK; +), using BNIP3L/Nix (D4R4B) Rabbit mAb. The BNIP3L/Nix construct was kindly provided by Dr. Reuben Shaw, Salk Institute for Biological Studies, La Jolla, CA.
Immunoprecipitation of BNIP3L/Nix from A172 cells, treated with cobalt chloride (100 μM, overnight), using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or BNIP3L/Nix (D4R4B) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using BNIP3L/Nix (D4R4B) Rabbit mAb.
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).
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For Research Use Only. Not For Use In Diagnostic Procedures.