Analytical Data
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Gene name
KLK7
- Application
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Alternative Names
KLK7；PRSS6；SCCE；Kallikrein-7
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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
P49862
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Expression Region
30-253aa
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AA Sequence
IIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVHLGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVKKVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKVYKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQPNDPGVYTQVCKFTKWINDTMKKHR
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Molecular Weight
30.4 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
KLK7, or Kallikrein-related peptidase 7, is a member of the kallikrein family of serine proteases, which are known to play crucial roles in various physiological processes, including tissue remodeling, inflammation, and cancer progression. Research into KLK7 has gained momentum due to its association with several malignancies, particularly in breast and prostate cancers, where its overexpression has been linked to tumorigenesis and metastasis. The enzyme is believed to degrade extracellular matrix components and activate other proteases, contributing to the invasive characteristics of malignant cells. Additionally, KLK7 is implicated in skin physiology, influencing keratinocyte differentiation and wound healing. The study of KLK7, especially in the context of recombinant protein production, has the potential to uncover its functional mechanisms and therapeutic applications. By utilizing techniques in molecular biology, researchers aim to produce KLK7 in a recombinant form to facilitate detailed biochemical studies. Understanding the structure-function relationship of KLK7 could provide insights into its role in disease processes and may reveal novel targets for drug development, particularly in cancer therapeutics. Overall, KLK7 represents a significant biomarker and potential therapeutic target, and ongoing research continues to focus on elucidating its precise role in health and disease.
