Recombinant Human Glyoxalase I Protein Summary
| Description |
An un-tagged recombinant protein corresponding to amino acids 1-184 of Human GLO1. Source: E.coli Amino Acid Sequence: MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM |
| Source |
E. coli |
| Protein/Peptide Type |
Recombinant Protein |
| Gene |
GLO1 |
| Purity |
>90%, by SDS-PAGE |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
20.7 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 |
1.0 mg/ml |
| Purity |
>90%, by SDS-PAGE |
Alternate Names for Recombinant Human Glyoxalase I Protein
Background
Glyoxalase I, also known as GLO1, belongs to the glyoxalase-i family. Glyoxalase I is responsible for the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutathione.This enzyme is ubiquitously expressed and is also present in many tumor cell lines, in which its concentration is often upregulated. Recombinant human GLO1 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 1 year from date of receipt.
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