Analytical Data
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基因名
CLEC2D
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简介
The OCIL/CLEC2D protein, also known as osteoclast inhibitory lectin (OCIL) or C-type lectin domain family 2 member D (CLEC2D), functions as a lectin-type receptor located on the cell surface. Lectins are proteins that specifically bind to carbohydrates, and OCIL/CLEC2D is involved in carbohydrate recognition and signaling processes by acting as a lectin-type receptor. OCIL/CLEC2D Protein, Rat (HEK293, Fc) is the recombinant rat-derived OCIL/CLEC2D protein, expressed by HEK293 , with N-hFc labeled tag.
- Application
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别名
C-type lectin domain family 2 member D5; Osteoclast inhibitory lectin; Ocil; Clec2d5
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种属
Rat
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表达系统
HEK293
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标签
N-hFc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q925N7
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表达区间
K98-L233
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蛋白长度
Extracellular Domain
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分子量
43-55 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
CLEC2D is a member of the C-type lectin receptor family, which plays a crucial role in immune responses and cell signaling. Recent studies have highlighted its importance in various biological processes, including the regulation of dendritic cell function and T cell activation. Research indicates that CLEC2D is involved in mediating interactions between immune cells and pathogens, influencing both adaptive and innate immunity. Its unique structure, characterized by a carbohydrate recognition domain, allows it to bind specific glycoconjugates on the surface of pathogens, which is essential for initiating immune responses. Given its pivotal role in the immune system, CLEC2D is considered a potential target for therapeutic interventions in autoimmune diseases, infections, and cancer. Understanding the structure-function relationship of CLEC2D through advanced techniques like X-ray crystallography and molecular modeling is critical for designing novel drugs that can modulate its activity. Continued research into CLEC2D will not only enhance our knowledge of immune regulation but also pave the way for innovative strategies in immunotherapy and vaccine development, making it a significant focus in current biomedical research.
