Recombinant Human Bag1 protein is a Human Fragment protein, in the 72 to 345 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, WB.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
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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).
HAP, BAG1, BAG family molecular chaperone regulator 1, BAG-1, Bcl-2-associated athanogene 1
Recombinant Human Bag1 protein is a Human Fragment protein, in the 72 to 345 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, WB.
pH: 7.5
Preservative: 1.02% Imidazole
Constituents: 25% Glycerol (glycerin, glycerine), 1.045% MOPS, 0.87% Sodium chloride, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00174% PMSF
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).
Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.
Bag1 protein also known as Bcl-2-associated athanogene 1 has a molecular mass of approximately 46 kDa. The protein is ubiquitously expressed in various tissues and cells indicating its broad functional significance. Bag1 serves as a co-chaperone interacting directly with heat shock protein 70 (Hsp70) to modulate its activity. This interaction affects the protein folding process ensuring cellular proteins maintain their proper conformation.
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.
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.
Dysregulation of Bag1 connects to cancer development and neurodegenerative diseases. Overexpression of Bag1 has associations with cancers such as breast cancer where it promotes tumor growth by inhibiting apoptosis. Bag1's ability to interact with the Bcl-2 protein makes it a significant player in cancer pathways. Additionally changes in Bag1 expression and function have been observed in Alzheimer's disease highlighting its role in neuron survival and stress response. Bag1's involvement with proteins like Hsp70 and Bcl-2 highlights its potential as a therapeutic target in these conditions.
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SDS-PAGE showing ab85158 at approximately 66kDa.
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