Recombinant Human Glutaredoxin 1/GLRX1 Protein Summary
Description |
An un-tagged recombinant protein corresponding to the amino acids1-106 of Human Glutaredoxin 1/GLRX1 Source: E.coli Amino Acid Sequence: MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein |
Gene |
GLRX |
Purity |
>95%, by SDS-PAGE |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
11.7 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 10% glycerol |
Preservative |
No Preservative |
Concentration |
1 mg/ml |
Purity |
>95%, by SDS-PAGE |
Alternate Names for Recombinant Human Glutaredoxin 1/GLRX1 Protein
Background
Description: Glutaredoxin(GRX), also known as thioltransferase, is member of the thiol-disulfide oxidoreductase family. Glutraredoxin catalyzes the reversible reduction of protein-glutathionyl mixed disulfides to free sulfhydryl groups though a monothiol mechanism. Mammalian Glutaredoxin is known to have two isoforms, GRX1 and GRX2. GRX1 is a cytosolic protein, whereas GRX2 is localized both in the mitochondria and nucleus. Glutaredoxin-1 may be involved in a various cellular events such as signal transduction, stress response, and metabolic regulation by regulating the redox status of cellular proteins. Recombinant human Glutaredoxin1 protein was expressed in E.coli and purified by using conventional chromatography techniques.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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