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CE40
Recombinant Human BAG family molecular chaperone regulator 2/BAG2
10ug
1200
1080
现货
国产
-
CE40
Recombinant Human BAG family molecular chaperone regulator 2/BAG2
50ug
3520
3168
现货
国产
-
CE40
Recombinant Human BAG family molecular chaperone regulator 2/BAG2
500ug
12320
11088
现货
国产
-
CE40
Recombinant Human BAG family molecular chaperone regulator 2/BAG2
1mg
17600
15840
现货
国产
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Catalog# CE40 Source E. coli Description Recombinant Human BAG Family Molecular Chaperone Regulator 2/BAG2 is produced by our E. coli expression system. The target protein is expressed with sequence (Met1-Asn211) of Human BAG2 fused with a 6His tag at the N-terminus. Names BAG Family Molecular Chaperone Regulator 2, BAG-2, Bcl-2-Associated Athanogene 2, BAG2 Accession # O95816 Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0 Shipping The product is shipped at ambient temperature. Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in 1X PBS.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.Purity Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. Endotoxin Less than 0.1 ng/μg (1 IEU/μg). Amino Acid Sequence MGSSHHHHHHSSGLVPRGSHMAQAKINAKANEGRFCRSSSMADRSSRLLESLDQLELRVEALREA ATAVEQEKEILLEMIHSIQNSQDMRQISDGEREELNLTANRLMGRTLTVEVSVETIRNPQQQESL KHATRIIDEVVNKFLDDLGNAKSHLMSLYSACSSEVPHGPVDQKFQSIVIGCALEDQKKIKRRLE TLLRNIENSDKAIKLLEHSKGAGSKTLQQNAESRFNBackground BAG Family Molecular Chaperone Regulator 2 (BAG2) is a member of the Bag family whose members compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. BAG2 contains 1 BAG domain and is a important component of the HSC 70/CHIP chaperone-dependent ubiquitin ligase complex. In mammalian cells BAG1, BAG2, and BAG3 bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.