Analytical Data
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Gene name
FPR3
- Application
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Alternative Names
FPR3; FPRH1; FPRL2; N-formyl peptide receptor 3; FMLP-related receptor II; FMLP-R-II; Formyl peptide receptor-like 2
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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
P25089
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Expression Region
254-353aa
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AA Sequence
WFPYELIGILMAVWLKEMLLNGKYKIILVLINPTSSLAFFNSCLNPILYVFMGRNFQERLIRSLPTSLERALTEVPDSAQTSNTDTTSASPPEETELQAM
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Molecular Weight
36.63 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
FPR3, or formyl peptide receptor 3, is a member of the G-protein coupled receptor (GPCR) family, which plays a crucial role in immune responses and inflammation. Its primary function involves mediating the chemotaxis of immune cells, particularly neutrophils, towards sites of infection or injury through the recognition of formylated peptides produced by bacteria or damaged tissues. Research has increasingly highlighted FPR3's potential in modulating inflammatory responses and its involvement in various pathological conditions, including autoimmune diseases and cancer. The ability to manipulate FPR3 signaling pathways opens avenues for therapeutic interventions aimed at enhancing immune responses or controlling excessive inflammation. Moreover, recent studies have indicated that FPR3 may interact with other receptor systems, suggesting a more complex role in immune regulation than previously understood. The production and characterization of recombinant FPR3 proteins have become essential for elucidating its structure-function relationship and developing potent ligands. This research not only provides insights into FPR3's biological significance but also presents opportunities for the design of novel therapeutic agents targeting this receptor to improve clinical outcomes in various diseases. Understanding the molecular mechanisms governing FPR3 activity could enhance our capability to harness its functions for better health management.
