Analytical Data
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Gene name
PIR
- Application
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Alternative Names
PIR;Pirin
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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
O00625
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Expression Region
1-290aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSSKKVTLSVLSREQSEGVGARVRRSIGR PELKNLDPFLLFDEFKGGRPGGFPDHPHRGFETVSYLLEGGSMAHEDFCG HTGKMNPGDLQWMTAGRGILHAEMPCSEEPAHGLQLWVNLRSSEKMVEPQ YQELKSEEIPKPSKDGVTVAVISGEALGIKSKVYTRTPTLYLDFKLDPGA KHSQPIPKGWTSFIYTISGDVYIGPDDAQQKIEPHHTAVLGEGDSVQVEN KDPKRSHFVLIAGEPLREPVIQHGPFVMNTNEEISQAILDFRNAKNGFER AKTWKSKIGN
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Molecular Weight
34 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
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.
