Analytical Data
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Gene name
GZMA/Granzyme A
- Application
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Alternative Names
CTLA3; HFSP; HF; H factor; Granzyme 1; Fragmentin-1; Hanukkah factor; Cytotoxic T-Lymphocyte-Associated Serine Esterase 3; CTL tryptase; Cytotoxic T-lymphocyte proteinase 1
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Species
Mouse
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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
P11032
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Expression Region
Ile29~Val260
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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 A (GZMA) is a serine protease predominantly produced by cytotoxic T cells and natural killer (NK) cells, playing a crucial role in the immune response against tumors and virally infected cells. This enzyme is released in granules and enters target cells, where it induces apoptosis through specific cleavage of substrates. Research into GZMA has gained momentum due to its potential as both a therapeutic target and a biomarker in cancer immunotherapy. Its unique mechanism of action, distinct from other granzyme family members, has led to increased interest in understanding its function and regulation in immune responses. Recombinant GZMA protein production is essential for elucidating its biological properties, studying its interactions with various cellular pathways, and developing GZMA-based therapeutic strategies. Moreover, insights into its structure-function relationship can facilitate the design of inhibitors that modulate its activity, offering a novel approach to enhance cancer treatment or tailor immune responses. As research progresses, GZMA may become a critical player in the development of innovative immunotherapeutic approaches, contributing to more effective strategies against malignancies and infectious diseases.
