Analytical Data
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基因名
CRIP2
- Application
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别名
Protein ESP1
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种属
Human
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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
P52943
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表达区间
1-208aa
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分子量
38.5 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
CRIP2 (Cysteine-Rich Protein 2) is a member of the CRIP family of proteins, which are known to play significant roles in cellular processes, including cell growth, differentiation, and response to environmental stresses. Research into CRIP2 has gained traction due to its potential implications in various physiological and pathological contexts, particularly in the development of cardiac and skeletal muscle tissues. Given that CRIP2 contains multiple cysteine-rich motifs, its interactions with metal ions and potential involvement in redox regulation have drawn attention. Studies have suggested that CRIP2 may be implicated in the modulation of signaling pathways linked to oxidative stress and apoptosis, making it a candidate for investigation in diseases such as cancer and heart failure. As a recombinant protein, CRIP2 can be expressed and purified for in vitro studies, enabling researchers to elucidate its biochemical properties, functional roles, and interactions with other proteins. Understanding CRIP2's structure-function relationship is crucial for determining its exact contributions to cellular mechanisms and its potential as a therapeutic target. Thus, the study of CRIP2 not only enhances our comprehension of basic biological functions but may also lead to advancements in disease treatment and the development of novel biomolecular applications.
