Analytical Data
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Gene name
PI
- Application
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Alternative Names
PI；CRISP9；PSPBP；Peptidase inhibitor 16
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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
P01009
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Expression Region
1-418aa
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AA Sequence
MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
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Molecular Weight
46.7 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
PI protein, or Phosphoinositide, is a crucial component involved in various cellular processes, including signal transduction, membrane dynamics, and cytoskeletal rearrangements. The study of PI recombinant proteins has become increasingly important due to their roles in cellular signaling pathways that mediate responses to external stimuli, such as growth factors and hormones. Research has shown that alterations in PI signaling can lead to various diseases, including cancer, diabetes, and neurological disorders, making it vital to understand these pathways at a molecular level. The production of recombinant PI proteins allows for detailed studies of their structure and function, facilitating the identification of specific interaction partners and downstream effects. Techniques such as molecular cloning and expression systems, including bacteria, yeast, and mammalian cells, have enabled researchers to generate these proteins in sufficient quantities for functional assays and structural analyses. Additionally, the development of novel purification methods has improved the yield and activity of recombinant PI proteins, opening up new avenues for therapeutic intervention. Ongoing research aims to decipher the complex networks regulated by PI proteins, contributing to a better understanding of cellular homeostasis and the potential development of isoform-specific drugs to target PI-related pathologies. Thus, the exploration of PI recombinant proteins holds significant promise for both basic research and clinical applications.
