BCL2/adenovirus E1B 19kDa Interacting Protein 1 (BNIP1) (AA 52-174) antibody

Details for Product No. ABIN968362
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Antigen
Synonyms NIP1, SEC20, TRG-8, 2010005M06Rik, 5930429G21Rik, Sec20, 2900010M17Rik, AI853434, Apba2bp, Nip1, XB51
Epitope
AA 52-174
(10), (8), (3), (3), (3), (2), (2), (1), (1), (1), (1), (1)
Reactivity
Human
(53), (19), (17), (12), (12), (12)
Host
Mouse
(40), (9), (5)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(3), (3), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunofluorescence (IF)
(44), (21), (10), (9), (5), (3), (2), (1), (1), (1)
Pubmed 3 references available
Quantity 50 µg
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Catalog No. ABIN968362
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Immunogen Human Nip1
Clone 5
Isotype IgG1
Cross-Reactivity Rat (Rattus)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Nip1
Background Apoptosis, a selective process of genetically programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. In addition, apoptotic programs in virus-infected cells regulate viral replication and pathogenesis. However, viruses, such as human adenovirus, have evolved methods of circumventing these programs. The adenovirus E1B region encodes a 19 kDa protein (19K) that, similar to Bcl-2, suppresses apoptosis via interactions with intracellular proteins such as Bcl-2 family members. In addition, 19K and Bcl-2 interact with members of a novel subfamily of pro-apoptotic proteins which includes Nip1-3 and Nix. These proteins contain C-terminal transmembrane (TM) domains, such as those found in Bcl-2 proteins. The TM domain is important for targeting of proteins to mitochondria and nuclear envelope/ER regions of the cell. More specifically, Nip1 localizes at the nuclear envelope/ER, while Nip3 localizes in mitochondria and other cytoplasmic membrane structures. In addition, Nip1 shares homology with the catalytic domain of mammalian calcium/calmodulin-dependent cyclic nucleotide phosphodiesterases (PDEs) and may have a PDE-like activity.
Molecular Weight 26 kDa
Comment

Related Products: ABIN968533, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-BCL2/adenovirus E1B 19kDa Interacting Protein 1 (BNIP1) (AA 52-174) antibody Immunofluorescence staining of human fibroblasts.
anti-BCL2/adenovirus E1B 19kDa Interacting Protein 1 (BNIP1) (AA 52-174) antibody (2) Western blot analysis of Nip1 on a A431 cell lysate (Human epithelial carcinoma, ATCC CRL-1555). Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the mouse anti-Nip1 antibody.
anti-BCL2/adenovirus E1B 19kDa Interacting Protein 1 (BNIP1) (AA 52-174) antibody (3) anti-BCL2/adenovirus E1B 19kDa Interacting Protein 1 (BNIP1) (AA 52-174) antibody (Image 3)
Product cited in: Boyd, Malstrom, Subramanian et al.: "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins." in: Cell, Vol. 79, Issue 2, pp. 341-51, 1994 (PubMed).

Yasuda, Theodorakis, Subramanian et al.: "Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence." in: The Journal of biological chemistry, Vol. 273, Issue 20, pp. 12415-21, 1998 (PubMed).

Chen, Cizeau, Vande Velde et al.: "Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins." in: The Journal of biological chemistry, Vol. 274, Issue 1, pp. 7-10, 1999 (PubMed).

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