Analytical Data
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基因名
TRIM34
- Application
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别名
TRIM34; IFP1; RNF21; Tripartite motif-containing Protein 34; Interferon-responsive finger Protein 1; RING finger Protein 21
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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
Q9BYJ4
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表达区间
1-488 aa
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氨基酸序列
MASKILLNVQ EEVTCPICLE LLTEPLSLDC GHSLCRACIT VSNKEAVTSM GGKSSCPVCG ISYSFEHLQA NQHLANIVER LKEVKLSPDN GKKRDLCDHH GEKLLLFCKE DRKVICWLCE RSQEHRGHHT VLTEEVFKEC QEKLQAVLKR LKKEEEEAEK LEADIREEKT SWKYQVQTER QRIQTEFDQL RSILNNEEQR ELQRLEEEEK KTLDKFAEAE DELVQQKQLV RELISDVECR SQWSTMELLQ DMSGIMKWSE IWRLKKPKMV SKKLKTVFHA PDLSRMLQMF RELTAVRCYW VDVTLNSVNL NLNLVLSEDQ RQVISVPIWP FQCYNYGVLG SQYFSSGKHY WEVDVSKKTA WILGVYCRTY SRHMKYVVRR CANRQNLYTK YRPLFGYWVI GLQNKCKYGV FEESLSSDPE VLTLSMAVPP CRVGVFLDYE AGIVSFFNVT SHGSLIYKFS KCCFSQPVYP YFNPWNCPAP MTLCPPSS
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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
TRIM34, a member of the tripartite motif (TRIM) protein family, is gaining attention due to its potential roles in various cellular processes, including immune response, apoptosis, and cell proliferation. Research indicates that TRIM proteins are involved in the regulation of protein stability and the modulation of signaling pathways, making them crucial players in maintaining cellular homeostasis. TRIM34 has been implicated in the regulation of innate immunity and may play a role in the response to viral infections. Studies suggest that it may interact with other proteins to form complexes that influence the transcriptional activity of key immune-related genes. Given the increasing interest in the therapeutic potential of manipulating TRIM proteins for treating diseases such as cancer and autoimmune disorders, understanding the specific functions and mechanisms of TRIM34 is vital. Investigating the structural features of TRIM34, including its E3 ligase activity, could provide insights into its functional role in disease contexts and highlight possible avenues for drug development. The ongoing research aims to elucidate these aspects, with the hope of translating findings into practical applications in clinical settings.
