Analytical Data
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Gene name
KLK11
- Application
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Alternative Names
KLK11；PRSS20；TLSP；Kallikrein-11
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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
Q9UBX7
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Expression Region
19-250aa
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AA Sequence
IIKGFECKPHSQPWQAALFEKTRLLCGATLIAPRWLLTAAHCLKPRYIVH LGQHNLQKEE GCEQTRTATESFPHPGFNNSLPNKDHRNDIMLVKMASPVSITWAVRPLTL SSRCVTAGTS CLISGWGSTSSPQLRLPHTLRCANITIIEHQKCENAYPGNITDTMVCASV QEGGKDSCQG DSGGPLVCNQSLQGIISWGQDPCAITRKPGVYTKVCKYVDWIQETMKNNV DHHHHHH
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Molecular Weight
25 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
KLK11, or kallikrein-related peptidase 11, is a member of the kallikrein family of serine proteases, which play crucial roles in various biological processes including coagulation, inflammation, and tissue remodeling. Research on KLK11 has gained attention due to its potential implications in cancer biology, particularly in prostate cancer and ovarian cancer, where alterations in its expression levels have been correlated with disease progression and prognosis. Additionally, KLK11 has been identified as a potential biomarker for certain pathological conditions, as well as a target for therapeutic interventions. Recent advancements in recombinant protein technology have facilitated the production of KLK11 in a suitable format for functional studies, enabling researchers to explore its enzymatic activities, substrate specificities, and regulatory mechanisms. This has opened new avenues for understanding the physiological and pathological roles of KLK11, including its involvement in cell signaling pathways and its interplay with other proteases in the tumor microenvironment. As research progresses, KLK11 continues to be investigated for its full potential in clinical applications, both as a diagnostic tool and as a therapeutic target, paving the way for novel strategies in cancer treatment and precision medicine.
