Analytical Data
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Gene name
KLK14
- Application
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Alternative Names
KLK14；KLKL6；Kallikrein-14
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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
Q9P0G3
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Expression Region
41-267aa
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AA Sequence
IIGGHTCTRS SQPWQAALLA GPRRRFLCGG ALLSGQWVIT AAHCGRPILQ VALGKHNLRR WEATQQVLRV VRQVTHPNYN SRTHDNDLML LQLQQPARIG RAVRPIEVTQ ACASPGTSCR VSGWGTISSP IARYPASLQC VNINISPDEV CQKAYPRTIT PGMVCAGVPQ GGKDSCQGDS GGPLVCRGQL QGLVSWGMER CALPGYPGVY TNLCKYRSWI EETMRDK
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Molecular Weight
29.1 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
KLK14, also known as kallikrein-related peptidase 14, is a member of the human kallikrein gene family, which plays significant roles in various physiological processes, including tissue remodeling, inflammation, and cancer progression. Research into KLK14 has intensified due to its potential implications in diseases such as breast cancer and other malignancies, where it is often dysregulated. The proteolytic activity of KLK14 facilitates the cleavage of various biomolecules, thereby influencing the tumor microenvironment and metastatic behavior of cancer cells. Advances in recombinant protein technology have enabled the production of active KLK14 for biochemical characterization and therapeutic exploration. Studies have demonstrated that elevated KLK14 levels correlate with poor prognosis and may serve as a novel biomarker for tumor aggressiveness. The investigation of KLK14 as a therapeutic target is particularly appealing, given its specific expression patterns in cancerous tissues compared to normal tissues. Current research focuses on elucidating the substrate specificity of KLK14, understanding its regulatory mechanisms, and exploring its role in the tumorigenic process, which could lead to the development of KLK14-based diagnostic tools and targeted therapies. Overall, the study of KLK14 not only enhances our understanding of kallikrein biology but also opens new avenues for translational research in oncology.
