Recombinant Human Bag1 protein (Tag Free)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human Bag1 protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB.
View Alternative Names
HAP, BAG1, BAG family molecular chaperone regulator 1, BAG-1, Bcl-2-associated athanogene 1
- WB
Unknown
Western blot - Recombinant Human Bag1 protein (Tag Free) (AB93929)
All lanes:
Anti-Bag1 antibody (<a href='/en-us/products/unavailable/bag1-antibody-ab7976'>ab7976</a>) at 1 µg/mL
All lanes:
Western blot - Recombinant Human Bag1 protein (Tag Free) (ab93929) at 0.001 µg
Secondary
All lanes:
Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution
true
Exposure time: 10s
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Bag1 protein (AB93929)
15% SDS-PAGE showing ab93929 (3 μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Bag1 plays essential roles in regulating cell survival and apoptosis. It can exist as part of a larger protein complex and is known to bind with the anti-apoptotic protein Bcl-2 enhancing cell survival. By interacting with these proteins Bag1 helps control the delicate balance between cell death and survival critical for normal cellular function and response to stress. Bag1 also affects transcription regulation cell cycle progression and cellular response to stress stimuli.
Pathways
Bag1 integrates into cellular stress response and apoptotic signaling pathways. Bag1's interaction with Hsp70 associates it with the heat shock response pathway which upregulates molecular chaperones to protect cells during stress. Additionally its binding to Bcl-2 situates it within the apoptotic pathway where it supports cell survival by inhibiting caspase activation. The protein further interacts with key regulatory proteins like Raf-1 linking it to the MAPK/ERK signaling pathway involved in cell growth and division.
Specifications
Form
Liquid
Additional notes
Purified by using conventional chromatography techniques.
General info
Function
Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70 (PubMed : 24318877, PubMed : 27474739, PubMed : 9873016). Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity (PubMed : 12724406). Markedly increases the anti-cell death function of BCL2 induced by various stimuli (PubMed : 9305631). Involved in the STUB1-mediated proteasomal degradation of ESR1 in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury (By similarity).
Post-translational modifications
Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.
Subcellular localisation
Nucleus
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com