Analytical Data
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Gene name
GGH
- Application
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Alternative Names
GGH;Gamma-glutamyl hydrolase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92820
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Expression Region
25-318aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMRPHGDTAKKPIIGILMQKCRNKVMKNYGR YYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLR RSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTAT DTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKN FTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWK NLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPI YTGNISSFQQCYIFD
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Molecular Weight
36 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The research on GGH (Gamma-Glutamyl Hydrolase) recombinant protein has emerged from the growing interest in understanding its biochemical role in various physiological processes. GGH is an enzyme that plays a crucial part in the metabolism of glutathione, a vital antioxidant in the human body. Its primary function includes the hydrolysis of gamma-glutamyl bonds in peptides and proteins, which is essential for the regulation of glutathione levels and the detoxification of harmful compounds. Abnormal GGH activity has been linked to several pathological conditions, including neurodegenerative diseases and cancer, highlighting the need for further investigation. The ability to produce GGH as a recombinant protein allows researchers to study its structure-function relationships, enzyme kinetics, and potential therapeutic applications in greater detail. Advances in genetic engineering and protein expression systems have facilitated the production of high-purity recombinant GGH, enabling more accurate biochemical assays and functional studies. Moreover, understanding GGH's molecular interactions can lead to the development of novel drugs that target its enzymatic activity, offering new avenues for treatment in diseases where glutathione metabolism is disrupted. Thus, the exploration of GGH recombinant protein is not only pivotal for fundamental biochemical research but also holds promise for innovative therapeutic strategies.
