Analytical Data
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基因名
OS9
- Application
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别名
OS9；Protein OS-9
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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
Q13438
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表达区间
1-612aa
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氨基酸序列
MAAETLLSSLLGLLLLGLLLPASLTGGVGSLNLEELSEMRYGIEILPLPV MGGQSQSSDVVIVSSKYKQRYECRLPAGAIHFQREREEETPAYQGPGIPE LLSPMRDAPCLLKTKDWWTYEFCYGRHIQQYHMEDSEIKGEVLYLGYYQS AFDWDDETAKASKQHRLKRYHSQTYGNGSKCDLNGRPREAEVRFLCDEGA GISGDYIDRVDEPLSCSYVLTIRTPRLCPHPLLRPPPSAAPQAILCHPSL QPEEYMAYVQRQADSKQYGDKIIEELQDLGPQVWSETKSGVAPQKMAGAS PTKDDSKDSDFWKMLNEPEDQAPGGEEVPAEEQDPSPEAADSASGAPNDF QNNVQVKVIRSPADLIRFIEELKGGTKKGKPNIGQEQPVDDAAEVPQREP EKERGDPERQREMEEEEDEDEDEDEDEDERQLLGEFEKELEGILLPSDRD RLRSEVKAGMERELENIIQETEKELDPDGLKKESERDRAMLALTSTLNKL IKRLEEKQSPELVKKHKKKRVVPKKPPPSPQPTGKIEIKIVRPWAEGTEE GARWLTDEDTRNLKEIFFNILVPGAEEAQKERQRQKELESNYRRVWGSPG GEGTGDLDEFDF
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分子量
96 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
OS9 (Oligosaccharyl site 9) is a key player in the folding and maturation of glycoproteins within the endoplasmic reticulum (ER). It functions as a lectin that recognizes and binds to misfolded glycoproteins, thereby facilitating their retrotranslocation to the cytosol for degradation via the ubiquitin-proteasome system. This process is crucial for cellular quality control, as the accumulation of misfolded proteins can lead to various diseases, including neurodegenerative disorders and cancers. Research on OS9 has gained momentum due to its potential role in understanding the mechanisms underlying these diseases and its implications in therapeutic strategies targeting protein misfolding. Furthermore, studies have highlighted the involvement of OS9 in regulating ER-stress responses and its interactions with other molecular chaperones. The elucidation of OS9’s structure and function could provide insights into its mechanism of action, enhance our understanding of ER-associated degradation (ERAD), and open avenues for drug development aimed at modulating OS9 activity. Overall, the investigation of OS9 is significant not only for basic biological research but also for the development of novel approaches to treat conditions resulting from protein misfolding and aggregation.
