Analytical Data
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Gene name
Kallikrein-11
- Application
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Alternative Names
TLSP; hK11; Hippostatin; Kallikrein-Related Peptidase 11; Serine protease 20; Trypsin-like protease
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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
Q9UBX7
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Expression Region
Ile39~Asn282
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Molecular Weight
30.5kDa
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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-11 (KLK11) is a member of the kallikrein family of serine proteases, which play critical roles in various physiological processes, including blood pressure regulation, reproductive functions, and cancer progression. Research on KLK11 has garnered attention due to its potential involvement in cancer biology, particularly in prostate and ovarian cancers, where abnormal expression levels have been linked to tumorigenesis and metastasis. The interest in KLK11 extends beyond cancer, as it may also play a role in regulating inflammation and neurodegenerative disorders. As a glycosylated protein, KLK11's structure is complex, involving post-translational modifications that influence its activity and stability. Given its physiological significance, the production of recombinant KLK11 protein is pivotal for studying its biochemical properties and elucidating its functions. Overcoming challenges in expression, purification, and activity assessment is essential for advancing our understanding of KLK11's roles in health and disease. Investigating recombinant KLK11 not only contributes to the fundamental knowledge of kallikrein-related proteases but also has potential implications for therapeutic strategies aimed at targeting KLK11 in pathological conditions. Overall, KLK11 represents a fascinating subject for further exploration in protease research.
