Analytical Data
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基因名
SRPRB
- Application
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别名
SRPRB；Signal recognition particle receptor subunit beta
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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
Q9Y5M8
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表达区间
1-271aa
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氨基酸序列
MASADSRRVADGGGAGGTFQPYLDTLRQELQQTDPTLLSVVVAVLAVLLTLVFWKLIRSRRSSQRAVLLVGLCDSGKTLLFVRLLTGLYRDTQTSITDSCAVYRVNNNRGNSLTLIDLPGHESLRLQFLERFKSSARAIVFVVDSAAFQREVKDVAEFLYQVLIDSMGLKNTPSFLIACNKQDIAMAKSAKLIQQQLEKELNTLRVTRSAAPSTLDSSSTAPAQLGKKGKEFEFSQLPLKVEFLECSAKGGRGDVGSADIQDLEKWLAKIA
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分子量
29.7 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
SRPRB (Signal Recognition Particle Receptor Subunit Beta) is a critical protein involved in the cellular mechanism of co-translational translocation of proteins into the endoplasmic reticulum (ER). Research on SRPRB has gained attention due to its essential role in protein synthesis and maturation, which are vital for maintaining cellular homeostasis and function. The protein works in conjunction with the Signal Recognition Particle (SRP), facilitating the correct targeting and insertion of nascent polypeptides into the ER membrane. Misfunctionalities or mutations in SRPRB are linked to various diseases, including neurodegenerative disorders and certain cancers, highlighting its importance in health and disease contexts. Advances in structural biology and biochemistry have provided insights into the molecular architecture and dynamics of SRPRB, paving the way for potential therapeutic interventions. As researchers continue to explore the complexities of protein interactions and translocation mechanisms, understanding SRPRB's function at a molecular level may unlock novel strategies for drug design and treatment of diseases associated with protein misfolding and malfunction. Thus, the study of SRPRB is not only crucial for basic biological research but also holds significant promise for translational applications in medicine.
