Analytical Data
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Gene name
Kallikrein-2
- Application
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Alternative Names
KLK2A2; HK2; Prostatic Kallikrein-Related Peptidase 2; Glandular kallikrein-1; Tissue kallikrein-2
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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
P20151
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Expression Region
Pro19~Pro261
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Molecular Weight
32kDa
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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
Kallikrein-2 (KLK2) is a serine protease belonging to the kallikrein family, which has garnered significant attention due to its potential roles in various physiological and pathological processes, particularly in cancer biology. Elevated levels of KLK2 have been associated with prostate cancer progression, making it a candidate biomarker for diagnosis and prognosis. Furthermore, KLK2 is involved in the regulation of extracellular matrix components and inflammation, which are critical in tumor microenvironments. The study of KLK2 has been propelled by advancements in recombinant DNA technology, enabling the production of KLK2 recombinant proteins for in-depth analysis of its functions, regulatory mechanisms, and interactions with other proteins. Investigating KLK2 may provide insights into its enzymatic activity, substrate specificity, and potential therapeutic applications, including the development of KLK2 inhibitors that could modulate its activity in cancer treatment. As research continues to unravel the complex roles of KLK2 in disease, the recombinant protein serves as a valuable tool for elucidating its biological relevance and therapeutic potentials.
