Analytical Data
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基因名
Klk1b22
- Application
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别名
Beta-NGF-endopeptidase;Epidermal growth factor-binding protein type A ;EGF-BP AGlandular kallikrein K22 ;mGK-22Nerve growth factor beta chain endopeptidaseTissue kallikrein 22
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种属
Mouse
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P15948
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表达区间
25-259aa
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分子量
41.8 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
Klk1b22 is a member of the kallikrein-related peptidase family, which is known for its role in various physiological processes, including blood pressure regulation, inflammation, and tissue remodeling. The gene encoding Klk1b22 is located in a cluster on mouse chromosome 7 and has been shown to be expressed predominantly in the reproductive tissues, particularly in the prostate and seminal vesicles. Its specific functions, however, remain largely unexplored. The study of Klk1b22 recombinant protein is significant for several reasons. Firstly, understanding its substrate specificity and enzymatic activity could provide insights into its biological roles and potential implications in health and disease, particularly in hormone-related disorders. Additionally, given the structural similarities to other kallikreins, Klk1b22 may serve as a model for investigating the regulatory mechanisms governing the kallikrein family, which has been implicated in several pathological conditions, including cancer. Nevertheless, further research is necessary to elucidate its precise functions and to explore its potential as a biomarker or therapeutic target. Thus, the generation and characterization of Klk1b22 recombinant protein represent a crucial step in advancing our knowledge of this enigmatic protease and its contributions to both normal physiology and disease states.
