Analytical Data
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基因名
TRIM5
- Application
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别名
TRIM5；RNF88；Tripartite motif-containing Protein 5
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9C035
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表达区间
1-493aa
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氨基酸序列
MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDK GESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGE KLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLR QKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNEL QNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGV DGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVD VTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILG SQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYW VIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVS FFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS
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分子量
70 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
TRIM5α is a member of the TRIM (tripartite motif-containing) protein family, known for its role in the innate immune response against retroviral infections, particularly HIV-1. The protein possesses a unique tripartite structure that comprises a RING finger domain, a B-box, and a coiled-coil region, enabling it to recognize and bind to the viral capsid. This interaction initiates a series of antiviral responses, including the recruitment of cellular factors that induce degradation of the viral RNA and protein, thereby limiting viral replication. Research on TRIM5α has expanded to explore its polymorphisms and how variations in the protein may confer differential susceptibility to viral infections among different populations. Additionally, findings have suggested that TRIM5α may have broader implications beyond retroviral defense, potentially influencing various cellular processes such as inflammation and tumor suppression. Recent advances in structural biology and mutagenesis have provided valuable insights into the mechanisms underlying its antiviral activity, leading to potential therapeutic applications in combating retroviral diseases. The exploration of TRIM5α and its variants thus comprises a significant area of study within virology and immunology, with hopes of harnessing its properties for novel antiviral strategies.
