Recombinant e.coli grxB protein
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Recombinant e.coli grxB protein
Description:
GrxB (Glutaredoxin-2) belongs to the glutaredoxin family. Glutaredoxins are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. This protein involved in reducing some disulfides in a coupled system with glutathione reductase. It does not act as hydrogen donor for ribonucleotide reductase. Recombinant E. coli grxB protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.Product Name Alternative:
Glutaredoxin 2 (Grx2), glutaredoxin 2, Grx2, bA101E13.1, CGI-133, GRLX2Expression System:
E.coliAntigen Species:
E.coliTag:
His-TagApplications:
SDS-PAGEConcentration:
1 mg/mL (determined by Bradford assay)Purity:
> 95% by SDS-PAGEMolecular Weight:
26.5 kDa (235aa) confirmed by MALDI-TOFAdditionnal Information:
GrxB, glutaredoxin 2 (Grx2), glutaredoxin 2, Grx2, bA101E13.1, CGI-133, GRLX2, ATGP1040-10 µg, ATGP1040-20 µg, ATGP1040-50 µg, ATGP1040-100 µg, ATGP1040-250 µg, ATGP1040-500 µg, ATGP1040-1 mg, ATGP1040-10, ATGP1040-20, ATGP1040-50, ATGP1040-100, ATGP1040-250, ATGP1040-500, ATGP1040-1References & Citations:
Holmgren A, et al. (2004) Antioxid. Redox. Signal. 6 (1) : 63-74.; ; Lopez-Maury L, et al. (2009) J Bacteriol. 191 (11) :3534-43.Storage Conditions:
Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.Formulation:
Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 50 mM NaClScientific Category:
Redox ProteinsNCBI Accession Number:
NP_415582Uniprot Accession Number:
P0AC59Species:
E.coliAA Sequence:
MGSSHHHHHH SSGLVPRGSH MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI LQKDDSRYMP ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL LLPRFAKSAF DEFSTPAARK YFVDKKEASA GNFADLLAHS DGLIKNISDD LRALDKLIVK PNAVNGELSE DDIQLFPLLR NLTLVAGINW PSRVADYRDN MAKQTQINLL SSMAI
