Analytical Data
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Gene name
PRSS50
- Application
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Alternative Names
TSP50; CT20; Cancer/Testis Antigen 20; Testes Specific Protease 50; Testis-specific protease-like protein 50
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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 90% as determined by SDS-PAGE.
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Uniprot
Q9UI38
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Expression Region
Ala40~Leu385
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Molecular Weight
43kDa
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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
Related Products
Protein Description
PRSS50, a member of the serine protease family, has garnered attention in recent years due to its potential roles in various physiological and pathological processes. Its expression pattern is notably rich in reproductive tissues, suggesting a possible function in fertility and gametogenesis. Research indicates that PRSS50 may influence sperm maturation or fertilization, although the precise mechanisms remain largely unexplored. Moreover, preliminary studies have indicated that aberrant PRSS50 expression could be linked to certain cancers, prompting further investigation into its role in tumor biology. Understanding the structural and functional aspects of PRSS50 through recombinant protein studies could provide insights into its enzymatic activity, substrate specificity, and overall biological significance. This research is vital, as it could lead to the development of novel therapeutic strategies targeting PRSS50-related pathways in reproductive health and cancer. By elucidating the functional dynamics of this protease, scientists aim to reveal its potential as a biomarker or therapeutic target, ultimately contributing to advancements in clinical applications and improved patient outcomes.
