Analytical Data
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Gene name
KLK8
- Application
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Alternative Names
KLK8；NRPN；PRSS19；TADG14；Kallikrein-8
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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
O60259
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Expression Region
29-260aa
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AA Sequence
QEDKVLGGHECQPHSQPWQAALFQGQQLLCGGVLVGGNWVLTAAHCKKPK YTVRLGDHSLQNKDGPEQEIPVVQSIPHPCYNSSDVEDHNHDLMLLQLRD QASLGSKVKPISLADHCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKI FPQKKCEDAYPGQITDVMVCAGSSKGADTCQGDSGGPLVCDGALQGITSW GSDPCGRSDKPGVYTNICRYLDWIKKIIGSKG
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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
KLK8, also known as kallikrein-related peptidase 8, is a member of the human kallikrein gene family, which consists of serine proteases involved in various physiological processes, including protein catabolism, immune response, and tissue remodeling. The study of KLK8 has garnered significant attention due to its potential role in various diseases, particularly in cancer and inflammatory conditions. Elevated levels of KLK8 have been associated with certain malignant tumors, making it a candidate for diagnostic and prognostic biomarkers. Furthermore, the exploration of KLK8 as a therapeutic target has led to interest in the development of recombinant KLK8 proteins for use in research and clinical applications. These recombinant proteins facilitate the elucidation of KLK8's biochemical properties, regulatory mechanisms, and its interactions with other proteins. Understanding KLK8's structure-function relationships and its involvement in disease pathways can provide insights into new treatment strategies and improve disease management. Overall, the research on KLK8 recombinant proteins represents a promising area of study with the potential to contribute significantly to the fields of cancer research and therapeutic development.
