Analytical Data
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Gene name
Granzyme H/GZMH
- Application
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Alternative Names
CCP-X; CGL-2; CSP-C; CTLA1; CTSGL2; Cathepsin G-Like 2,Protein h-CCPX; Cytotoxic T-lymphocyte proteinase; Cytotoxic serine protease C
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P20718
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Expression Region
Glu19~Leu246
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Molecular Weight
29kDa
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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
Granzyme H (GZMH) is a serine protease that belongs to the granzyme family, primarily expressed in cytotoxic T lymphocytes and natural killer (NK) cells. It plays a significant role in the immune response by inducing apoptosis in target cells, particularly virally infected or tumor cells. Research has highlighted GZMH's unique substrate specificity and its distinct role compared to other granzymes, making it a focus of immunological studies, especially in the context of cancer immunotherapy and viral infections. The recombinant production of GZMH has enabled researchers to investigate its biochemical properties, cellular functions, and interactions with various substrates. Studying GZMH can provide critical insights into the mechanisms of immune evasion used by tumors and pathogens, offering potential therapeutic targets for enhancing immune responses in cancer treatment and improving antiviral strategies. The ongoing investigation of GZMH in both basic and applied research aims to elucidate its role in the immune system and explore its potential as a biomarker or therapeutic agent.











