Analytical Data
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基因名
PIR
- Application
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别名
PIR;Pirin
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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
O00625
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表达区间
1-290aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMGSSKKVTLSVLSREQSEGVGARVRRSIGR PELKNLDPFLLFDEFKGGRPGGFPDHPHRGFETVSYLLEGGSMAHEDFCG HTGKMNPGDLQWMTAGRGILHAEMPCSEEPAHGLQLWVNLRSSEKMVEPQ YQELKSEEIPKPSKDGVTVAVISGEALGIKSKVYTRTPTLYLDFKLDPGA KHSQPIPKGWTSFIYTISGDVYIGPDDAQQKIEPHHTAVLGEGDSVQVEN KDPKRSHFVLIAGEPLREPVIQHGPFVMNTNEEISQAILDFRNAKNGFER AKTWKSKIGN
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分子量
34 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
PIR (Protein Interaction Regulator) proteins play a crucial role in various cellular processes by modulating protein-protein interactions. Understanding the structure and function of PIR proteins has become a significant area of research due to their involvement in essential biological pathways, including signal transduction, cell cycle regulation, and metabolic processes. Mutations or dysregulation of these proteins have been linked to numerous diseases, including cancer and neurodegenerative disorders. Recent advancements in proteomics and structural biology, such as X-ray crystallography and cryo-electron microscopy, have enabled scientists to elucidate the intricate mechanisms by which PIR proteins interact with their partners and influence cellular functions. This knowledge not only contributes to our understanding of fundamental biological processes but also opens avenues for therapeutic interventions targeting aberrant PIR protein interactions. Overall, the study of PIR proteins is essential for unraveling complex biological networks and developing novel strategies for disease treatment and prevention.
