Recombinant Human UBE2A Protein, His-tagged


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Recombinant Human UBE2A Protein, His-tagged

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Cat.No. : UBE2A-530H
Product Overview : Recombinant Human UBE2A (Accession # NP_003327), fused with an N-terminal 6-His tag, was produced in E. coli.
Source : E. coli
Species : Human
Tag : His
Form : X mg/ml (XµM) in 50 mM HEPES pH 7.5, 200 mM NaCl, 10% Glycerol (v/v), 1 mM TCEP
Bio-activity : Recombinant Human His6-HR6A/UBE2A is a member of the Ubiquitin-conjugating (E2) enzyme family that receives Ubiquitin from a Ubiquitin-activating (E1) enzyme and subsequently interacts with a Ubiquitin ligase (E3) to conjugate Ubiquitin to substrate proteins. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human His6-HR6A/UBE2A concentration of 0.1-1 µM.
Molecular Mass : Recombinant Human UBE2A, His-tagged has a calculated MW of 19 kDa.
Purity : >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Storage : Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at: In lyophilized state for 1 year (4ºC); After reconstitution under sterile conditions for 3 months (-70ºC).
Reconstitution : Reconstitute at 10 µg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Gene Name : UBE2A ubiquitin-conjugating enzyme E2A [ Homo sapiens ]
Official Symbol : UBE2A
Synonyms : UBE2A; ubiquitin-conjugating enzyme E2A; ubiquitin conjugating enzyme E2A (RAD6 homolog); ubiquitin-conjugating enzyme E2 A; HHR6A; RAD6A; UBC2; HR6A; RAD6 homolog A; ubiquitin-protein ligase A; ubiquitin carrier protein A; ubiquitin-conjugating enzyme E2A (RAD6 homolog); MRXSN; MRXS30;
Gene ID : 7319
mRNA Refseq : NM_003336
Protein Refseq : NP_003327
MIM : 312180
UniProt ID : P49459
Chromosome Location : Xq24
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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