Analytical Data
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基因名
SIGLEC1
- Application
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别名
pSn;Sialic acid-binding Ig-like lectin 1;Siglec-1;p210
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种属
Pig
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
A7LCJ3
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表达区间
20-153aa
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分子量
22.3 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
SIGLEC1 (Sialic Acid Binding Immunoglobulin-like Lectin 1), also known as sialoadhesin, is a type of cell surface receptor predominantly expressed on macrophages and dendritic cells. It plays a crucial role in the immune system by recognizing sialylated glycoproteins and glycolipids, which are often found on the surface of pathogenic organisms and infected cells. The study of SIGLEC1 has garnered attention due to its potential implications in various diseases, including infections, cancers, and autoimmune disorders. Researchers have been exploring the functional aspects of SIGLEC1, investigating how its binding mechanisms can influence immune responses and contribute to the regulation of inflammation. Additionally, there has been a growing interest in developing SIGLEC1 recombinant proteins for therapeutic applications, such as targeted drug delivery and as biomarkers for disease diagnosis. The engineering of SIGLEC1 as a recombinant protein allows for detailed studies of its structure-function relationships and opens avenues for using it in the development of novel immunotherapies, aimed at modulating immune responses for disease treatment. Understanding the complexities of SIGLEC1 interactions at the molecular level is essential for harnessing its potential in clinical applications and advancing our knowledge of immune system regulation.
