KLK10 Human, Sf9
Description
Production and Purification
The protein is purified via affinity chromatography using its His6 tag and formulated in 30% glycerol, 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, and 1 mM DTT for stability . Long-term storage recommendations include adding carrier proteins (e.g., 0.1% HSA or BSA) to prevent aggregation .
Anti-Inflammatory and Atheroprotective Effects
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Endothelial Protection: Recombinant KLK10 (rKLK10) inhibits NFκB activation, reduces VCAM1/ICAM1 expression, and suppresses monocyte adhesion in human aortic endothelial cells (HAECs) exposed to TNFα or oscillatory shear stress .
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In Vivo Efficacy: Intravenous administration of rKLK10 (0.6 mg/kg) decreases arterial inflammation in murine models, with dose-dependent suppression of atherosclerotic plaque formation .
Tumor-Suppressive Roles
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Cancer Biology: KLK10 is implicated in suppressing tumorigenesis in breast and prostate cancers, though mechanistic details remain under investigation .
Applications in Biomedical Research
KLK10 Human, Sf9 is utilized in:
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Drug Development: Preclinical studies targeting atherosclerosis and inflammatory diseases .
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Mechanistic Studies: Elucidating KLK10’s protease-dependent signaling pathways, particularly its interaction with PAR1/PAR2 receptors .
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Diagnostics: Potential biomarker exploration in cancers (e.g., ovarian, lung) .
Challenges and Future Directions
While KLK10 Human, Sf9 shows promise, challenges include optimizing its pharmacokinetics (e.g., short plasma half-life of 4.5 hours) and clarifying its tumor-suppressive mechanisms. Ongoing research focuses on engineering fusion proteins (e.g., Fc-KLK10) to enhance stability and delivery .
Product Specs
Kallikrein-10, also known as KLK10, is a serine protease belonging to the kallikrein subfamily. This subfamily, comprising 15 members, is clustered on chromosome 19. Kallikreins play diverse roles in physiological processes. KLK10, a secreted protein, is notable for its potential tumor-suppressing properties in breast and prostate cancers.
Recombinant KLK10, expressed in Sf9 insect cells using a baculovirus system, is a single polypeptide chain with glycosylation. It encompasses amino acids 34 to 276, totaling 252 amino acids, and possesses a molecular weight of 27.8 kDa. This protein is engineered with a 6-amino acid His-tag at its C-terminus to facilitate purification, which is achieved through standard chromatographic techniques.
The KLK10 protein solution is provided at a concentration of 0.5 mg/ml and is formulated in a buffer consisting of 30% glycerol, 20 mM Tris-HCl at a pH of 8.0, 0.15 M NaCl, and 1 mM DTT.
The purity of KLK10 is determined to be greater than 90% using SDS-PAGE analysis.
Sf9, Baculovirus cells.
ADPALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSNHHHH HH.
Product Science Overview
Kallikrein-10 (KLK10) is a member of the kallikrein subfamily of serine proteases, which are enzymes that cleave peptide bonds in proteins. The kallikrein family consists of 15 members, each encoded by a gene located in a cluster on chromosome 19q13.4 . KLK10 is also known by several other names, including Kallikrein-Related Peptidase 10, PRSSL1, NES1 (Normal Epithelial Cell-Specific 1), and Breast Normal Epithelial Cell Associated Serine Protease .
KLK10 is secreted and plays a significant role in various physiological processes. It has been implicated in the suppression of tumorigenesis, particularly in breast and prostate cancers . The physiological functions of many kallikreins, including KLK10, are still being elucidated, but they are known to participate in proteolytic cascades, which are sequences of enzymatic reactions that lead to the breakdown of proteins .
KLK10 is expressed in a variety of tissues and biological fluids. It is highly expressed in certain tissues, such as the prostate, but is also found at lower concentrations in a wide range of other tissues . The expression patterns of KLK10 and other kallikreins can provide clues about their physiological roles and potential involvement in disease processes .
KLK10 can be produced recombinantly using the Sf9 insect cell line, which is derived from the fall armyworm Spodoptera frugiperda. The recombinant KLK10 produced in Sf9 cells is a single, glycosylated polypeptide chain containing 252 amino acids and has a molecular mass of 27.8 kDa . This recombinant protein is often fused to a His-Tag at the C-terminus to facilitate purification by standard chromatography techniques .
Recombinant KLK10 has various applications in research and clinical settings. It is used to study the enzyme’s structure and function, investigate its role in cancer and other diseases, and develop potential therapeutic interventions. The availability of recombinant KLK10 allows researchers to conduct experiments that would be difficult or impossible with native protein extracted from tissues.
