儲(chǔ)存: -15°C to -25°C/1 year(Do not lower than -25°C)
克隆性: Monoclonal
克隆號(hào): PT0437R
特異性: Endogenous
基因名稱(chēng): BAG3
蛋白名稱(chēng): BAG family molecular chaperone regulator 3
別名: BAG3;BIS;BAG family molecular chaperone regulator 3;BAG-3;Bcl-2-associated athanogene 3;Bcl-2-binding protein Bis;Docking protein CAIR-1
Organism-1: Human
基因ID-1: 9531
SwissProt-1: O95817
Organism-2: Mouse
基因ID-2: 29810
SwissProt-2: Q9JLV1
背景: 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. [provided by RefSeq, Jul 2008],
儲(chǔ)存: -15°C to -25°C/1 year(Do not lower than -25°C)
克隆性: Monoclonal
克隆號(hào): PT0437R
特異性: Endogenous
基因名稱(chēng): BAG3
蛋白名稱(chēng): BAG family molecular chaperone regulator 3
別名: BAG3;BIS;BAG family molecular chaperone regulator 3;BAG-3;Bcl-2-associated athanogene 3;Bcl-2-binding protein Bis;Docking protein CAIR-1
Organism-1: Human
基因ID-1: 9531
SwissProt-1: O95817
Organism-2: Mouse
基因ID-2: 29810
SwissProt-2: Q9JLV1
背景: 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. [provided by RefSeq, Jul 2008],