Analytical Data
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基因名
IL-13Rα2
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简介
IL-13R alpha 2 Protein, acting as a monomer, displays a strong binding affinity for interleukin-13 (IL-13). IL-13R alpha 2 Protein, Mouse (HEK293, His-Fc) is the recombinant mouse-derived IL-13R alpha 2 protein, expressed by HEK293 , with C-hFc, C-His labeled tag.
- Application
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别名
Interleukin-13 receptor subunit alpha-2; IL-13R-alpha-2; IL-13RA2; CD213a2; IL13RA2; IL13R
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种属
Mouse
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表达系统
HEK293
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标签
C-hFc;C-His
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纯度
> 90% as determined by SDS-PAGE.
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蛋白编号
O88786
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表达区间
L22-K334
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蛋白长度
Extracellular Domain
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分子量
75-80 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
IL-13Rα2 (Interleukin-13 receptor alpha 2) is a receptor for interleukin-13 (IL-13), a cytokine implicated in various inflammatory and fibrotic diseases, as well as in tumor biology. The overexpression of IL-13Rα2 has been observed in several cancers, making it a potential target for therapeutic intervention. Unlike its counterpart IL-13Rα1, which participates in mediating IL-13 signaling leading to beneficial immune responses, IL-13Rα2 lacks a functional signaling domain and acts primarily as a decoy receptor, sequestering IL-13 and limiting its availability to IL-13Rα1. This paradoxical role urges the exploration of IL-13Rα2 as a biomarker for tumor progression and an attractive candidate for targeted therapies, including antibody-drug conjugates and adoptive cell therapies. Researchers have been developing recombinant forms of IL-13Rα2 to study its structure and function, as well as to explore its potential in diagnostic and therapeutic applications. These recombinant proteins enable investigations into binding affinities, receptor dimerization, and downstream signaling pathways, providing insights into how IL-13Rα2 modulates tumor microenvironments and influences immune responses. Understanding IL-13Rα2's role in both normal physiology and pathology is essential for harnessing its potential in clinical applications, thereby advancing cancer treatment strategies and improving patient outcomes.
