Analytical Data
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基因名
SRP72
- Application
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别名
SRP72；Signal recognition particle subunit SRP72
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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
O76094
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表达区间
2-671aa
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氨基酸序列
ASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLYRLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPENLGLQEGTHELCYNTACALIGQGQLNQAMKILQKAEDLCRRSLSEDTDGTEEDPQAELAIIHGQMAYILQLQGRTEEALQLYNQIIKLKPTDVGLLAVIANNIITINKDQNVFDSKKKVKLTNAEGVEFKLSKKQLQAIEFNKALLAMYTNQAEQCRKISASLQSQSPEHLLPVLIQAAQLCREKQHTKAIELLQEFSDQHPENAAEIKLTMAQLKISQGNISKACLILRSIEELKHKPGMVSALVTMYSHEEDIDSAIEVFTQAIQWYQNHQPKSPAHLSLIREAANFKLKYGRKKEAISDLQQLWKQNPKDIHTLAQLISAYSLVDPEKAKALSKHLPSSDSMSLKVDVEALENSAGATYIRKKGGKVTGDSQPKEQGQGDLKKKKKKKKGKLPKNYDPKVTPDPERWLPMRERSYYRGRKKGKKKDQIGKGTQGATAGASSELDASKTVSSPPTSPRPGSAATVSASTSNIIPPRHQKPAGAPATKKKQQQKKKKGGKGGW
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分子量
101.1 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
SRP72, a critical component of the Signal Recognition Particle (SRP) complex, plays a significant role in the co-translational targeting of nascent proteins to the endoplasmic reticulum (ER) in eukaryotic cells. The SRP pathway is crucial for the proper localization and function of membrane and secretory proteins, which are integral for maintaining cellular homeostasis and communication. Recent studies have highlighted the importance of SRP72 in modulating the efficiency of protein translocation and have also suggested that it could be involved in various cellular processes beyond protein targeting, including stress responses and transmembrane signaling. Given its pivotal role, SRP72 has emerged as a potential target for understanding diseases associated with protein misfolding and trafficking, such as neurodegenerative disorders and certain cancers. Research into the structure and function of SRP72, including its interactions within the SRP complex, is vital for unraveling the molecular mechanisms underpinning protein synthesis and trafficking. This knowledge could pave the way for novel therapeutic strategies aimed at correcting or mitigating the consequences of aberrant protein misfolding and secretion, thereby contributing to the development of interventions for a range of human diseases. As the scientific community continues to explore the versatile roles of SRP72, it holds promise for enhancing our understanding of cellular biology and the pathology of diseases linked to protein mismanagement.
