Analytical Data
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基因名
KLK4
- Application
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别名
KLK4；EMSP1；PRSS17；PSTS；Kallikrein-4
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y5K2
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表达区间
27-254aa
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氨基酸序列
SCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNS YTIGLGLHSL EADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSIS IASQCPTAGN SCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGG QDQKDSCNGD SGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQASVD HHHHHH
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分子量
25 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.
