BAG-3 Protein, Mouse (P.pastoris, His)

The BAG-3 protein is a co-chaperone of HSP70 and HSC70, acting as a nucleotide exchange factor to promote the release of ADP from these partners, thus triggering substrate release. BAG-3 Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived BAG-3 protein, expressed by P. pastoris , with N-His labeled tag.

The BAG-3 protein functions as a co-chaperone alongside HSP70 and HSC70 chaperone proteins, playing a pivotal role as a nucleotide-exchange factor (NEF). Its NEF activity facilitates the release of ADP from HSP70 and HSC70, triggering the liberation of client/substrate proteins. The nucleotide release is mediated through its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70, while substrate release is facilitated by its interaction with the substrate-binding domain (SBD) of HSPA8/HSC70. Beyond its role in chaperone activity, BAG-3 exhibits anti-apoptotic activity and is involved in the nucleocytoplasmic transport of HSF1. It binds to the ATPase domain of HSP70/HSC70 chaperones, interacts with BCL2, phospholipase C-gamma proteins, and DNAJB6. Furthermore, BAG-3 engages in interactions with HSF1, HSPA8, HSPA1A, and HSPA1B, and binds to SYNPO2 via its WW domain 1 and SYNPO2's PPPY motif, underscoring its versatile involvement in cellular processes and protein-protein interactions.

Mouse

P. pastoris

N-His

Q9JLV1 (S2-P577)

29810  [NCBI]

Full Length of Mature Protein

SAATQSPMMQMASGNGASDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPPEGPKDTASSANGPSRDGSRLLPIREGHPIYPQLRPGYIPIPVLHEGSENRQPHLFHAYSQPGVQRFRTEAAAATPQRSQSPLRGGMTEAAQTDKQCGQMPATATTAAAQPPTAHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYIPIPVIHEQNITRPAAQPSFHQAQKTHYPAQQGEYQPQQPVYHKIQGDDWEPRPLRAASPFRSPVRGASSREGSPARSGTPVHCPSPIRVHTVVDRPQPMTHREPPPVTQPENKPESKPGPAGPDLPPGHIPIQVIRREADSKPVSQKSPPPAEKVEVKVSSAPIPCPSPSPAPSAVPSPPKNVAAEQKAAPSPAPAEPAAPKSGEAETPPKHPGVLKVEAILEKVQGLEQAVDSFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKAIDVPGQVQVYELQPSNLEAEQPLQEIMGAVVADKDKKGPENKDPQTESQQLEAKAATPPNPSNPADSAGNLVAP

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.