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BAG-1M (human), (recombinant) (His-tag)

ADI-APR-400-0050 50 µg 204.00 USD
ADI-APR-400-0200 200 µg 503.00 USD
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Product Specification

Alternative Name:BCL2-associated athanogene
Recommended Dilutions/Conditions:Western Blot (100ng, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
MW:~46kDa (~51kDa observed with His-tag)
Source:Produced in E. coli. Human BAG-1M is fused at the N-terminus to a His-tag.
UniProt ID:Q99933
Formulation:Liquid. In 20mM TRIS-HCl, pH 7.5, containing 100mM sodium chloride, 1mM DTT, and 1% glycerol.
Purity:≥80% (SDS-PAGE; Western Blot)
Purity Detail:Purified by multi-step chromatography.
Application Notes:Western blot control.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Scientific Background:BAG-1 is a Bcl-2-binding protein which lacks sequence homology with Bcl-2 and its related proteins, and functions to enhance the anti-apoptotic effects of Bcl- 2. BAG-1 is expressed as three major functionally distinct and differentially localized isoforms, which originate from a single mRNA. BAG-1S, 36 kDa, typically found in cytoplasm, generally the most abundant isoform in normal cells; BAG-1M, 46 kDa, found in both the nucleus and cytoplasm and under certain conditions, it can translocate from cytoplasm to nucleus; and BAG-1L, 50 kDa, nuclear localized, involved in regulating transcription. BAG-1 binds to the intracellular domain of the hepatocyte growth factor (HGF) and platelet-derived growth factor (PDGF) receptors, enhancing growth factor mediated protection from apoptosis. BAG-1 binds to the ATPase domain of Hsc70/Hsp70 to modulate its chaperone activity, in-part regulating Raf-1 activity and the assembly of glucocorticoid receptors.
BAG-1M (human), (recombinant) (His-tag) ELISA
ELISA analysis of interaction between BAG-1M (human), (recombinant) (His-tag) (Prod. No. ADI-APR-400), BAG-1S (human), (recombinant) (His-tag) (GST-tag) (Prod. No. ADI-APR-401) and HSP70 (Prod. No. ADI-ESP-555). 2-Fold serial dilution of HSP70 from 38 μg/ml down to 0.58 ng/ml was incubated with plate pre-coated with 10μg of BAG-1M, BAG-1S or BSA. Bound HSP70 was probed with HSP70 mAb (Prod. No. ADI-SPA-810) followed by goat anti-mouse IgG, HRP-conjugated (Prod. No. ADI-SAB-100), and detected by TMB.
BAG-1M (human), (recombinant) (His-tag) Western blot
Western Blot analysis: Lane 1: MW marker, Lane 2: BAG-1M (human), (recombinant) (His-tag) (Prod. No. ADI-APR-400), Lane 3: BAG-1S (human), (recombinant) (His-tag) (GST-tag) (Prod. No. ADI-APR-401) probed with BAG-1, pAb (Prod. No. ADI-905-735).
BAG-1M (human), (recombinant) (His-tag) SDS-PAGE
SDS-PAGE analysis of BAG-1M (human), (recombinant) (His-tag) (Prod. No. ADI-APR-400): Lane 1: MW marker, Lane 2: 0.5μg, Lane 3: 1μg BAG-1M.
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BAG-1M (human), (recombinant) (His-tag) ELISA BAG-1M (human), (recombinant) (His-tag) Western blot BAG-1M (human), (recombinant) (His-tag) SDS-PAGE

Product Literature References

The BAG-1 isoform BAG-1M regulates keratin-associated Hsp70 chaperoning of aPKC in intestinal cells during activation of inflammatory signaling: A. Mashukova, et al.; J. Cell Sci. 127, 3568 (2014), Abstract; Full Text

General Literature References

BAG-1: a multi-functional pro-survival molecule: P.A. Townsend, et al.; Int. J. Biochem. Cell. Biol. 37, 251 (2005), Abstract;
Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery: K.C. Kanelakis, et al.; J. Biol .Chem. 274, 34134 (1999), Abstract;
BAG-1 modulates the chaperone activity of Hsp70/Hsc70: S. Takayama, et al.; EMBO J. 16, 4887 (1997), Abstract;
Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1: H.G. Wang, et al.; PNAS U.S.A. 93, 7063 (1996), Abstract;
HGF receptor associates with the anti-apoptotic protein BAG-1 and prevents cell death: A. Bardelli, et al.; EMBO J. 15, 6205 (1996), Abstract;
Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity: S. Takayama, et al.; Cell 80, 279 (1995), Abstract;

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