Analytical Data
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基因名
CLEC1B
- Application
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别名
1810061I13Rik; C type lectin domain family 1 member B; C type lectin like receptor 2; C-type lectin domain family 1 member B; C-type lectin domain family 1; member B; C-type lectin-like receptor
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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
Q9P126
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表达区间
1-196aa
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氨基酸序列
MQDEDGYITLNIKTRKPALVSAVMQRNYLQDENENRTGTLQQLAKRFCQYVVKQSELKGTFKGHKCSPCDTNWRYYGDSCYGFFRHNLTWEESKQYCTDMNATLLKIDNRNIVEYIKARTHLIRWVGLSRQKSNEVWKWEDGSVISENMFEFLEDGKGNMNCAYFHNGKMHPTFCENKHYLMCERKAGMTKVDQLP
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分子量
49.5 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
CLEC1B, also known as C-type lectin domain family 1 member B, is a key protein involved in the immune response, specifically in the recognition of pathogens and the regulation of immune cell functions. This protein is predominantly expressed in dendritic cells and macrophages, where it plays a crucial role in antigen presentation and the modulation of inflammatory responses. Research on CLEC1B has gained prominence due to its potential implications in various diseases, including infections, autoimmune disorders, and cancer. The unique structure of CLEC1B, characterized by its C-type lectin domain, allows it to interact with specific carbohydrate structures on pathogens, thereby influencing immune signaling pathways. Recent studies have focused on the functional characterization of CLEC1B to better understand its mechanisms in immune modulation and its potential as a therapeutic target. Investigating the pathways regulated by CLEC1B may provide insights into the development of novel immunotherapies and vaccines, highlighting its importance in both basic research and clinical applications. Overall, unlocking the functional roles of CLEC1B offers promising avenues for enhancing immune responses and addressing a range of health challenges.
