Analytical Data
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基因名
TMEM176B
- Application
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别名
TMEM176B; LR8; Transmembrane Protein 176B; Protein LR8
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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
Q3YBM2
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表达区间
1-270 aa
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氨基酸序列
MTQNTVIVNGVAMASRPSQPTHVNVHIHQESALTQLLKAGGSLKKFLFHPGDTVPSTARIGYEQLALGVTQILLGVVSCVLGVCLSLGPWTVLRASGCAFWAGSVVIAAGAGAIVHEKHPGKLAGYISSLLTLTGFATAMAAVVLCVNSFIWQTEPFLYIDTVCDRSDPVFPTTGYRWMRRSQENQWQKEECRAYMQMLRKLFTAIRALFLAVCVLKVIVSLVSLGVGLRNLCGQSSQPLNEEGSEKRLLGENSVPPSPSREQTSTAIVL
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分子量
55.6 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
TMEM176B, a member of the transmembrane protein family, has garnered attention in recent years due to its potential roles in human health and disease. Initially identified in immunological studies, TMEM176B is thought to be involved in the regulation of immune responses and may play a critical role in modulating cell signaling pathways. Research suggests that alterations in TMEM176B expression levels may be linked to various conditions, including autoimmune diseases and certain cancers, making it a candidate for further investigation. However, the precise biological functions and mechanisms of TMEM176B remain largely unexplored. To facilitate a deeper understanding of its role, the recombinant expression of TMEM176B has been pursued to produce purified protein for functional studies. This enables researchers to investigate its interactions with other cellular molecules and assess its impact on cellular processes. The study of TMEM176B recombinant protein could contribute valuable insights into its potential as a therapeutic target, offering possibilities for novel treatments in conditions associated with dysregulated immune responses and tumorigenesis. Overall, the exploration of TMEM176B at the molecular level represents a promising avenue for advancing our knowledge of its biological significance and therapeutic potential.












