Analytical Data
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基因名
SYVN1
- Application
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别名
E3 ubiquitin-protein ligase synoviolin. EC:2.3.2.27. RING-type E3 ubiquitin transferase synoviolin. Synovial apoptosis inhibitor 1
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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
Q86TM6
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表达区间
1-617 aa
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氨基酸序列
MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH
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分子量
94.1kDa
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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
SYVN1, or synoviolin-1, is an E3 ubiquitin ligase that plays a crucial role in protein quality control within the endoplasmic reticulum by mediating the ubiquitination and degradation of misfolded proteins. Its involvement in cellular processes, particularly in the regulation of protein homeostasis and apoptosis, has garnered significant attention in recent years. Dysregulation of SYVN1 has been implicated in various diseases, including cancer and neurodegenerative disorders. Research has shown that SYVN1 can influence the immune response and inflammation, making it a potential target for therapeutic intervention. The study of recombinant SYVN1 protein is vital for understanding its functional mechanisms and interactions with other cellular pathways. By generating and characterizing SYVN1 in a recombinant form, researchers aim to elucidate its structural properties and enzymatic activities, paving the way for the development of novel strategies aimed at modulating its function in disease contexts. Additionally, recombinant SYVN1 protein serves as a valuable tool for in vitro assays and screening for small-molecule inhibitors that could restore normal cellular function in SYVN1-related pathologies. This line of research holds promise not only for basic science understanding but also for potential clinical applications that could arise from targeting the SYVN1 pathway.
