中文名稱：BAG3抗原（重組蛋白）

英文名稱：BAG3 Antigen (Recombinant Protein)

儲(chǔ) 存：冷凍（-20℃）

相關(guān)類別：抗原

概述

Fusion protein corresponding to a region derived from 376-575 amino acids of human BAG3

技術(shù)規(guī)格

Full name:

BCL2 associated athanogene 3

Synonyms:

BIS; MFM6; BAG-3; CAIR-1

Swissprot:

O95817

Gene Accession:

BC014656

Purity:

>85%, as determined by Coomassie blue stained SDS-PAGE

Expression system:

Escherichia coli

Tags:

His tag C-Terminus, GST tag N-Terminus

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.

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021-54845833/15800441009

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BAG3抗原（重組蛋白）

Full name:	BCL2 associated athanogene 3
Synonyms:	BIS; MFM6; BAG-3; CAIR-1
Swissprot:	O95817
Gene Accession:	BC014656
Purity:	>85%, as determined by Coomassie blue stained SDS-PAGE
Expression system:	Escherichia coli
Tags:	His tag C-Terminus, GST tag N-Terminus
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.