Analytical Data
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Gene name
PIPPIN
- Application
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Alternative Names
Cold shock domain-containing protein C2. RNA-binding protein PIPPin
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y534
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Expression Region
1-153 aa
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AA Sequence
MTSESTSPPVVPPLHSPKSPVWPTFPFHREGSRVWERGGVPPRDLPSPLPTKRTRTYSATARASAGPVFKGVCKQFSRSQGHGFITPENGSEDIFVHVSDIEGEYVPVEGDEVTYKMCPIPPKNQKFQAVEVVLTQLAPHTPHETWSGQVVGS
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Molecular Weight
42.57 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
PIPPIN, a protein implicated in various cellular processes, has garnered significant interest in the field of molecular biology due to its potential roles in signal transduction and cellular communication. As a member of a specific protein family, PIPPIN is involved in the regulation of key physiological functions, including apoptosis and cell proliferation. Researchers have identified mutations and alterations in the expression of PIPPIN that are linked to various diseases, particularly cancer. This has prompted a concerted effort to understand its structural and functional characteristics through the study of its recombinant form. By creating recombinant PIPPIN, scientists aim to unravel its biological roles more effectively, assess its interactions with other cellular components, and explore its potential as a therapeutic target. The elucidation of PIPPIN's structure through techniques like X-ray crystallography and NMR spectroscopy is crucial for designing small molecules that could either mimic or inhibit its activity. Furthermore, understanding the molecular mechanisms underlying PIPPIN's function can provide insights into the development of novel strategies for disease intervention, thus highlighting the importance of recombinant protein studies in advancing biomedical research and therapeutic applications.
