Analytical Data
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基因名
TRAJ17
- Application
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别名
T cell receptor alpha joining 17
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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
A0A075B6W8
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表达区间
1-275 aa
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氨基酸序列
MASAPISMLAMLFTLSGLRAQSVAQPEDQVNVAEGNPLTVKCTYSVSGNPYLFWYVQYPNRGLQFLLKYITGDNLVKGSYGFEAEFNKSQTSFHLKKPSALVSDSALYFCAVRDAKAAGNKLTFGGGTRVLVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS
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分子量
56.8 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
TRAJ17 is a novel recombinant protein that has drawn significant attention in immunological research due to its potential role in adaptive immunity. Derived from the T cell receptor (TCR) gene locus, TRAJ17 is part of the diverse repertoire of TCR chains that facilitate recognition of specific antigens by T lymphocytes. Understanding the structure and function of TRAJ17 is crucial for uncovering its contributions to immune responses, particularly in the context of various diseases such as cancer, autoimmune disorders, and infectious diseases. The characterization of TRAJ17 and its interactions with other immune components can provide insights into T cell development and selection processes. Recent advancements in recombinant DNA technology enable the production of TRAJ17 in a laboratory setting, allowing for detailed studies of its biochemical properties, antigen-binding capabilities, and potential therapeutic applications. By examining how TRAJ17 influences T cell functionality, researchers aim to develop novel strategies for immunotherapy and vaccine design, harnessing the power of the immune system to enhance disease resistance and promote health. As such, TRAJ17 serves as a promising target for further investigation in the field of immunology, with implications that could extend to clinical practice and therapeutic innovations.
