Recombinant e.coli msrA protein

CAT: 0112-ATGP1036-100Size: 100 µgDry Ice: NoHazardous: No
CAT#:0112-ATGP1036-100Size:100 µg
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Description
Peptide methionine sulfoxide reductase A, also known msrA, is an enzyme that catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. This protein could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Recombinant E. coli msrA protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.
Product Name Alternative
Peptide methionine sulfoxide reductase A, ECK4215, JW4178, pms, pmsR, peptide-methionine (S) -S-oxide reductase
Expression System
E.coli
Antigen Species
E.coli
Tag
His-Tag
Applications
SDS-PAGE
Concentration
0.5 mg/mL (determined by Bradford assay)
Purity
> 90% by SDS-PAGE
Molecular Weight
25.4 kDa (232aa) confirmed by MALDI-TOF
Additionnal Information
MsrA, Peptide methionine sulfoxide reductase A, ECK4215, JW4178, pms, pmsR, peptide-methionine (S) -S-oxide reductase, ATGP1036-10 µg, ATGP1036-20 µg, ATGP1036-50 µg, ATGP1036-100 µg, ATGP1036-250 µg, ATGP1036-500 µg, ATGP1036-1 mg, ATGP1036-10, ATGP1036-20, ATGP1036-50, ATGP1036-100, ATGP1036-250, ATGP1036-500, ATGP1036-1
References & Citations
Kuschel L., et al. (1999) FEBS Letts.1:17-21.; ; Gabbita S., et al. (1999) J Neurochem. 4:1660-1666.
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, 0.1M NaCl
Scientific Category
Redox Proteins
NCBI Accession Number
NP_418640
Uniprot Accession Number
P0A744
Species
E.coli
AA Sequence
MGSSHHHHHH SSGLVPRGSH MSLFDKKHLV SPADALPGRN TPMPVATLHA VNGHSMTNVP DGMEIAIFAM GCFWGVERLF WQLPGVYSTA AGYTGGYTPN PTYREVCSGD TGHAEAVRIV YDPSVISYEQ LLQVFWENHD PAQGMRQGND HGTQYRSAIY PLTPEQDAAA RASLERFQAA MLAADDDRHI TTEIANATPF YYAEDDHQQY LHKNPYGYCG IGGIGVCLPP EA

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