Analytical Data
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Gene name
KLK4
- Application
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Alternative Names
KLK4；EMSP1；PRSS17；PSTS；Kallikrein-4
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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
Q9Y5K2
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Expression Region
27-254aa
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AA Sequence
SCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNS YTIGLGLHSL EADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSIS IASQCPTAGN SCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGG QDQKDSCNGD SGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQASVD HHHHHH
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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
KLK4, or Kallikrein-related peptidase 4, is a member of the kallikrein family of serine proteases, which play essential roles in various physiological and pathological processes, including tissue remodeling, inflammation, and cancer progression. Research has shown that KLK4 is upregulated in prostate cancer, making it a potential biomarker for diagnosis and a target for therapeutic intervention. The study of KLK4 recombinant proteins has gained interest due to their potential applications in understanding the enzyme's biological functions and its involvement in disease mechanisms. By producing KLK4 in a recombinant form, researchers can investigate its enzymatic activity, substrate specificity, and interactions with other biomolecules in a controlled environment. This approach facilitates the exploration of KLK4's role in cancer metastasis and its potential utility in clinical settings, such as the development of novel diagnostic tools or targeted therapies. Moreover, understanding the structure-function relationship of KLK4 through recombinant protein studies can provide insights into its regulatory mechanisms and the development of inhibitors that could mitigate its pathological effects. Overall, the investigation of KLK4 recombinant proteins represents a promising avenue for advancing our knowledge of this enzyme and its implications in health and disease.
