Analytical Data
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基因名
TRIM15
- Application
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别名
HGNC:16284; RING finger Protein 93; TRI15_HUMAN; TRIM15; Tripartite motif containing 15; Tripartite motif Protein 15; Tripartite motif-containing Protein 15; Zinc finger Protein 178; Zinc finger Protein B7; ZNF178; ZNFB7
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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
Q9C019
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表达区间
1-465 aa
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氨基酸序列
MPATPSLKVV HELPACTLCA GPLEDAVTIP CGHTFCRLCL PALSQMGAQS SGKILLCPLC QEEEQAETPM APVPLGPLGE TYCEEHGEKI YFFCENDAEF LCVFCREGPT HQAHTVGFLD EAIQPYRDRL RSRLEALSTE RDEIEDVKCQ EDQKLQVLLT QIESKKHQVE TAFERLQQEL EQQRCLLLAR LRELEQQIWK ERDEYITKVS EEVTRLGAQV KELEEKCQQP ASELLQDVRV NQSRCEMKTF VSPEAISPDL VKKIRDFHRK ILTLPEMMRM FSENLAHHLE IDSGVITLDP QTASRSLVLS EDRKSVRYTR QKKSLPDSPL RFDGLPAVLG FPGFSSGRHR WQVDLQLGDG GGCTVGVAGE GVRRKGEMGL SAEDGVWAVI ISHQQCWAST SPGTDLPLSE IPRGVRVALD YEAGQVTLHN AQTQEPIFTF TASFSGKVFP FFAVWKKGSC LTLKG
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分子量
52.1 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
TRIM15, a member of the TRIM (Tripartite Motif) family of proteins, has garnered attention in recent years due to its potential roles in immune response, cell differentiation, and various disease processes. TRIM proteins are characterized by the presence of a RING finger domain, a B-box, and a coiled-coil region, which contribute to their E3 ubiquitin ligase activity. Research has indicated that TRIM15 may be involved in regulating inflammatory pathways and modulating the innate immune response. Its expression patterns have been linked to various conditions, including autoimmune diseases and cancers. Studies have also suggested that TRIM15 interacts with critical signaling molecules, potentially influencing key biological processes such as cell proliferation and apoptosis. The detailed understanding of TRIM15’s functions and mechanisms could pave the way for novel therapeutic strategies aimed at targeting immune-related disorders and tumorigenesis. Ongoing research aims to elucidate its structure-function relationship and decipher the molecular pathways it influences, thereby providing insights into its role as a potential biomarker or therapeutic target in various diseases.
