recommended for detection of Bag-2 of mouse, rat, human and zebrafish origin by WB, IP, IF, IHC(P) and ELISA; also reactive with additional species, including canine
Bag-2 Background Information Bag-2 (Bcl-2-associated athanogene 2), also known as Bag family molecular chaperone regulator 2, is a member of the Bag family of proteins and contains the most diverged of the characteristic C-terminal Bag domain. Via their Bag domain, Bag proteins bind with high affinity to the HSC 70/HSP 70 ATPase domain, regulating chaperone activity and apoptosis. Bag-2 is an evolutionarily conserved cytoplasmic protein with putative N-terminal phosphorylation sites and specifically functions as an HSC 70 co-chaperone. Bag-2 is a major component of the HSC 70/CHIP chaperone-dependent ubiquitin ligase complex and acts to disrupt CHIP-mediated ubiquitylation. In this complex, Bag-2 directly interacts with the ATPase domain of HSC 70 as well as the U-box domain of CHIP and inhibits ubiquitylation by interfering with the association between CHIP and its ubiquitin conjugating enzyme.
Bag-2 (L-21)
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Bag-2 (L-21): sc-130969. Immunoperoxidase staining of formalin-fixed, paraffin-embedded human kidney tissue showing nuclear and cytoplasmic localization.
Bag-2 (L-21): sc-130969. Western blot analysis of Bag-2 expression in Jurkat whole cell lysate.
