BAG3 Polyclonal Antibody

Rs. 16,500.00
SKU E-AB-33621

Overview

Synonyms BAG 3,BAG family molecular chaperone regulator 3,BAG-3,Bag3,BAG3,Bcl 2 binding protein,Bcl-2-associated athanogene 3,Bcl-2-binding protein Bis,BCL2 associated athanogene 3,BCL2 binding athanogene 3,BIS,CAIR 1,Docking protein CAIR 1,Docking protein CAIR-1,MFM6
Swissprot O95817
Source Rabbit
Reactivity Human
Immunogen Synthesized peptide derived from the Internal region of human Bag-3.
Application WB,IHC-p,ELISA
Recommended dilution WB 1:500-1:2000, IHC 1:100-1:300, ELISA 1:5000-1:10000
Concentration 1mg/mL
Clonality Polyclonal

Properties

Cellular localization  
Tissue specificity  
Isotype IgG
Purification Affinity purification
Conjugation Unconjugated
Storage instructions Store at -20℃. Avoid freeze / thaw cycles.
Storage buffer PBS with 0.02% sodium azide, 0.5% BSA and 50% glycerol, pH7.4
Background 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. 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.

 

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