Analytical Data
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基因名
SCIN
- Application
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别名
Adseverin
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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
Q9Y6U3
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表达区间
1-715 aa
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氨基酸序列
MARELYHEEFARAGKQAGLQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKTSRGFTYHLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQNRELQGYESNDFVSYFKGGLKYKAGGVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEPSELIKVLGEKPELPDGGDDDDIIADISNRKMAKLYMVSDASGSMRVTVVAEENPFSMAMLLSEECFILDHGAAKQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKNTQIQVLPEGGETPIFKQFFKDWRDKDQSDGFGKVYVTEKVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIRVSQGKEPVHLLSLFKDKPLIIYKNGTSKKGGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPQNSGYIWVGKGASQEEEKGAEYVASVLKCKTLRIQEGEEPEEFWNSLGGKKDYQTSPLLETQAEDHPPRLYGCSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSKW
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分子量
88 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
The study of SCIN (Staphylococcal Complement Inhibitor) recombinant proteins has gained significant attention in recent years due to its critical role in the pathogenicity of Staphylococcus aureus, a leading cause of various infections in humans. SCIN is a 14-kDa protein that inhibits complement activation, thereby enhancing the survival of bacteria in the host immune response. Understanding the molecular structure and functions of SCIN can provide insights into its mechanisms of immune evasion, making it a potential target for novel therapeutic strategies. Researchers aim to produce recombinant SCIN proteins to study their properties and interactions with the immune system. By leveraging techniques such as recombinant DNA technology, scientists can produce large quantities of SCIN for in vitro and in vivo studies, facilitating the exploration of its effects on complement pathways and immune cell functions. Moreover, understanding SCIN's role in staphylococcal virulence can aid in the development of vaccines or inhibitors that counteract its immunosuppressive effects. The integration of SCIN studies with other areas of immunology and microbiology holds promise for the advancement of treatment options against infections caused by antibiotic-resistant strains of Staphylococcus aureus, addressing a pressing public health concern. Overall, the research on SCIN recombinant proteins not only enhances our knowledge of bacterial pathogenesis but also opens pathways for innovative therapeutic developments in combating bacterial infections.
