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BAG3

BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.
Protein class

Disease related genes, Human disease related genes, Plasma proteins

Predicted location

Intracellular

Single cell type specificity

Cell type enhanced (Basal prostatic cells, Urothelial cells, Basal squamous epithelial cells, Squamous epithelial cells)

Immune cell specificity

Immune cell enhanced (naive CD4 T-cell)

Cell line specificity

Low cell line specificity

Interaction

Binds to the ATPase domain of HSP70/HSC70 chaperones (PubMed:9873016). Interacts with BCL2 (PubMed:10597216). Interacts with phospholipase C-gamma proteins (PubMed:10980614). Interacts with DNAJB6 (PubMed:22366786). Interacts (via BAG domain) with HSF1; this interaction occurs in normal and heat-shocked cells promoting HSF1 nucleocytoplasmic shuttling (PubMed:26159920). Interacts with HSPA8 (via NBD) (PubMed:27474739, PubMed:24318877). Interacts with HSPA1A (via NBD) and HSPA1B (via NBD) (PubMed:24318877). Interacts (via WW domain 1) with SYNPO2 (via PPPY motif) (PubMed:23434281). Interacts with HSPB8 (PubMed:28144995).

Molecular function

Chaperone

More Types Infomation

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