Analytical Data
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基因名
PRNPIP
- Application
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别名
ERI3; PINT1; PRNPIP; PRNPIP1ERI1 exoribonuclease 3; EC 3.1.-.-; Prion interactor 1; Prion protein-interacting protein
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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
O43414
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表达区间
1-337 aa
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氨基酸序列
MATASPAADG GRGRPWEGGL VSWPPAPPLT LPWTWMGPSW GQHPGHWGFP ALTEPSASPA AGLGIFEVRR VLDASGCSML APLQTGAARF SSYLLSRARK VLGSHLFSPC GVPEFCSIST RKLAAHGFGA SMAAMVSFPP QRYHYFLVLD FEATCDKPQI HPQEIIEFPI LKLNGRTMEI ESTFHMYVQP VVHPQLTPFC TELTGIIQAM VDGQPSLQQV LERVDEWMAK EGLLDPNVKS IFVTCGDWDL KVMLPGQCQY LGLPVADYFK QWINLKKAYS FAMGCWPKNG LLDMNKGLSL QHIGRPHSGI DDCKNIANIM KTLAYRGFIF KQTSKPF
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分子量
37.2 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 PRNPIP protein, derived from the prion protein gene (PRNP), has garnered significant attention in the fields of molecular biology and neurodegenerative disease research. Prion diseases, characterized by misfolded proteins that lead to the aggregation of prion aggregates and neuronal damage, showcase the critical role of the prion protein in maintaining neuroprotective functions. Recent studies have highlighted that PRNPIP may play a significant role in the pathogenesis of these diseases, and its expression is linked to cellular stress responses and neuroprotection. Understanding the structure and function of PRNPIP is essential for elucidating its potential as a biomarker for prion diseases and as a target for therapeutic interventions. By employing techniques such as recombinant protein expression and purification, researchers aim to investigate the biochemical properties and interactions of PRNPIP with other cellular components. There is growing interest in exploring how modifications in PRNPIP expression affect neuronal health, neuronal survival, and prion propagation, which could pave the way for novel treatment strategies in prion-related disorders. The study of PRNPIP not only enhances our understanding of prion pathophysiology but also contributes to the broader field of protein misfolding diseases, offering insights into mechanisms that may be shared across various neurodegenerative conditions. Ultimately, elucidating the role of PRNPIP is crucial for developing innovative approaches to mitigate the debilitating effects of prion diseases and related disorders.
