Purity
Greater than 90% as determined by SDS-PAGE.
Alternative Names
HAGH; GLO2; HAGH1Hydroxyacylglutathione hydrolase; mitochondrial; EC 3.1.2.6; Glyoxalase II; Glx II
Species
Homo sapiens (Human)
Expression Region
50-308aa
Target Protein Sequence
KVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Tag Info
N-terminal GST-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that
we have in stock, however, if you have any special requirement for the format, please remark your
requirement when placing the order, we will prepare according to your demand.
Buffer
Tris-based buffer,50% glycerol
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw
cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature
and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized
form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description
In e.coli cells, the generation of recombinant Human HAGH protein involves cloning a DNA fragment encoding the Human HAGH protein (50-308aa) into a plasmid vector, which is then transferred into the e.coli cells. Positive cells are selected, cultured, and induced to express the HAGH protein. A N-terminal GST tag is attached to the protein. Lysis of the cells allows for the harvest of the recombinant Human HAGH protein. The collected recombiant Human HAGH protein is subjected to affinity purification and is identified using SDS-PAGE and subsequent staining of the gel with Coomassie Brilliant Blue. Its purity is greater than 90%.
