Analytical Data
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基因名
EPIM
- Application
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别名
STX2; EPIM; STX2A; STX2B; STX2C; Syntaxin-2; Epimorphin
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P32856
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表达区间
1-287aa
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氨基酸序列
MRDRLPDLTACRKNDDGDTVVVVEKDHFMDDFFHQVEEIRNSIDKITQYVEEVKKNHSIILSAPNPEGKIKEELEDLNKEIKKTANKIRAKLKAIEQSFDQDESGNRTSVDLRIRRTQHSVLSRKFVEAMAEYNEAQTLFRERSKGRIQRQLEITGRTTTDDELEEMLESGKPSIFTSDIISDSQITRQALNEIESRHKDIMKLETSIRELHEMFMDMAMFVETQGEMINNIERNVMNATDYVEHAKEETKKAIKYQSKARRKLMFIIICVIVLLVILGIILATTLS
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分子量
59.7 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
EPIM (epidermal growth factor-containing fibulin-like extracellular matrix protein) is a member of the fibulin family known for its role in the extracellular matrix, contributing to tissue function and integrity. Research into EPIM has gained traction due to its potential implications in various biological processes, including cellular adhesion, migration, and signaling pathways. Increased expression of EPIM has been linked to several pathological conditions, such as fibrosis and cancer, prompting scientists to investigate its molecular mechanisms and interactions. The study of EPIM recombinant proteins allows for a deeper understanding of its structure-function relationships and its role in disease processes. By utilizing techniques such as recombinant DNA technology, researchers can produce EPIM in a controlled environment, facilitating detailed biochemical analyses and functional assays. This not only furthers our understanding of EPIM itself but also paves the way for therapeutic applications, including targeted drug delivery and regenerative medicine. Continued exploration of EPIM and its recombinant forms holds promise for developing novel strategies to address various diseases linked to extracellular matrix dysregulation.
