Analytical Data
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基因名
FCAMR/CD351
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简介
FCAMR/CD351, functioning as a receptor, exhibits high-affinity binding to the Fc fragment of IgA and IgM. It plays a role in the immune response by mediating the endocytosis of IgA and IgM during the immune response to microbes. FCAMR/CD351 Protein, Mouse (HEK293, His) is the recombinant mouse-derived FCAMR/CD351 protein, expressed by HEK293 , with C-His labeled tag.
- Application
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别名
High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor; Fc alpha/mu receptor; uR
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种属
Mouse
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表达系统
HEK293
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标签
C-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q2TB54-2
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表达区间
M92-R511
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蛋白长度
Partial
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分子量
46.4 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
FCAMR/CD351 is a novel receptor that has garnered significant attention in immunological research due to its potential role in modulating immune responses. This receptor is primarily expressed on the surface of immune cells, such as B cells and antigen-presenting cells, suggesting its involvement in critical processes like antibody production and T cell activation. Studies indicate that FCAMR/CD351 may interact with various ligands, including IgA, pointing towards its function in facilitating mucosal immune responses. Its unique structure and expression patterns make it an intriguing target for understanding immune mechanisms and developing therapeutic strategies. Recent research has focused on characterizing the recombinant form of FCAMR/CD351, aiming to elucidate its functional properties and signaling pathways. This research is particularly important in the context of autoimmune diseases and infections, where enhancing or regulating immune responses could lead to novel treatment options. Furthermore, functional studies of this receptor could provide insight into its potential roles in vaccine development and cancer immunotherapy. Overall, the investigation of FCAMR/CD351 as a recombinant protein holds promise for advancing our understanding of immune regulation and developing new immunotherapeutic approaches.
