Analytical Data
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Gene name
KLK13
- Application
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Alternative Names
KLK13;KLKL4;Kallikrein-13
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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
Q9UKR3
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Expression Region
17-262aa
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AA Sequence
GGVSQESSKVLNTNGTSGFLPGGYTCFPHSQPWQAALLVQGRLLCGGVLV HPKWVLTAAHCLKEGLKVYLGKHALGRVEAGEQVREVVHSIPHPEYRRSP THLNHDHDIMLLELQSPVQLTGYIQTLPLSHNNRLTPGTTCRVSGWGTTT SPQVNYPKTLQCANIQLRSDEECRQVYPGKITDNMLCAGTKEGGKDSCEG DSGGPLVCNRTLYGIVSWGDFPCGQPDRPGVYTRVSRYVLWIRETIVDHH HHHH
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Molecular Weight
28 kDa
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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
KLK13, also known as kallikrein-related peptidase 13, is a member of the kallikrein family of serine proteases, which are implicated in various physiological processes, including inflammation, tissue remodeling, and cancer progression. Originally identified due to its aberrant expression in cancer tissues, KLK13 has garnered attention for its potential role as a biomarker for certain malignancies, particularly prostate cancer. Researchers have focused on the recombinant production of KLK13 to facilitate in-depth studies of its structure, function, and interactions with other proteins. By generating KLK13 in a controlled laboratory setting, scientists are able to analyze its enzymatic activity, substrate specificity, and regulatory mechanisms. Furthermore, understanding KLK13's involvement in proteolytic pathways may contribute insights into its potential therapeutic applications. Through the study of KLK13 and its recombinant form, the scientific community aims to elucidate its roles in tumor biology and explore its viability as a target for innovative cancer treatments, thereby advancing the field of oncological research and improving patient outcomes.
