Analytical Data
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Gene name
PIP
- Application
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Alternative Names
PIP;GCDFP15;GPIP4;Prolactin-inducible 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
P12273
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Expression Region
28-146aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSQDNTRKIIIKNFDIPKSVRPNDEVTAV LAVQTELKECMVVKTYLISSIPLQGAFNYKYTACLCDDNPKTFYWDFYTN RTVQIAAVVDVIRELGICPDDAAVIPIKNNRFYTIEILKVE
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Molecular Weight
16 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
Related Products
Protein Description
The study of PIP (Phosphoinositide-interacting protein) recombinant proteins has garnered significant interest due to their critical roles in cellular signaling and membrane dynamics. PIPs are known to participate in various biological processes, including cell growth, differentiation, and migration, by interacting with phosphoinositides and regulating multiple signaling pathways. The ability to produce recombinant PIP proteins has revolutionized research, enabling scientists to elucidate their functions in vitro and in vivo. By utilizing advanced techniques in molecular biology, such as recombinant DNA technology and expression systems, researchers can generate these proteins in a controlled manner, providing insights into their structure-function relationships. Investigating PIP proteins can lead to a better understanding of their mechanisms in health and disease, including cancer and metabolic disorders. By deciphering how PIPs modulate intracellular signaling, researchers aim to identify potential therapeutic targets and develop novel treatments. Thus, the exploration of PIP recombinant proteins not only enriches our fundamental knowledge of cell biology but also holds promise for translational applications in medicine.
