Analytical Data
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Gene name
PRNPIP
- Application
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Alternative Names
ERI3; PINT1; PRNPIP; PRNPIP1ERI1 exoribonuclease 3; EC 3.1.-.-; Prion interactor 1; Prion protein-interacting protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43414
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Expression Region
1-337 aa
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AA Sequence
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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Molecular Weight
37.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
