Recombinant Mouse Fmet-Leu-Phe Receptor (FPR1) Protein (His-GST&Myc)

Beta LifeScience SKU/CAT #: BLC-02211P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Fmet-Leu-Phe Receptor (FPR1) Protein (His-GST&Myc)

Beta LifeScience SKU/CAT #: BLC-02211P
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Product Overview

Description Recombinant Mouse Fmet-Leu-Phe Receptor (FPR1) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P33766
Target Symbol FPR1
Synonyms Fpr1; fMet-Leu-Phe receptor; fMLP receptor; N-formyl peptide receptor; FPR; N-formylpeptide chemoattractant receptor
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His-GST&C-Myc
Target Protein Sequence MDTNMSLLMNKSAVNLMNVSGSTQSVSAGYIVLDV
Expression Range 1-35aa
Protein Length Partial
Mol. Weight 33.7 kDa
Research Area Immunology
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors. Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing ROS release.
Subcellular Location Cell membrane; Multi-pass membrane protein.
Protein Families G-protein coupled receptor 1 family
Database References

KEGG: mmu:14293

STRING: 10090.ENSMUSP00000052894

UniGene: PMID: 28466255

  • the FPR1 downstream signaling pathways were competitively inhibited by HCH6-1. Furthermore, HCH6-1 prevented pulmonary neutrophil infiltration and edema along with alveolar damage in LPS-induced ALI in mice. Our findings suggest that HCH6-1, a FPR1 antagonist, may have potential as a new therapeutic agent for treating FPR1-involved inflammatory lung diseases PMID: 28232203
  • Intravital TPLSM revealed that formyl-peptide-FPR1 signaling is responsible for regulating neutrophil chemotaxis to allow migration into the necrotic area in hepatic ischemia-reperfusion injury PMID: 28062700
  • Formylated MHC class Ib binding peptides activate both human and mouse neutrophils primarily through FPR1. PMID: 27907124
  • Blocking of FPR1 completely abrogated the fMet-Leu-Phe-, gliadin- and synthetic peptide-induced migration. PMID: 26378785
  • these results highlight the importance of FPR1 in chemotherapy-induced anticancer immune responses. PMID: 26516201
  • Ovalbumininduced airway inflammation is mediated by upregulation of the TLR2/MyD88/NFkappaB signaling pathway and inhibition of LXA4R. PMID: 25760938
  • Deficiency of formyl peptide receptor 1 is associated with increased inflammation and enhanced liver injury after LPS-stimulation PMID: 24956481
  • these findings identify a novel role of FPR1 as pattern recognition receptors for perceiving the enteric microbiota that promotes repair of mucosal wounds via generation of reactive oxygen species from the enterocyte NOX1. PMID: 24192910
  • Further, these results reveal Fpr1 as a major mediator of host commensal interaction during dysbiosis. PMID: 24034617
  • The mechanism involved impaired early neutrophil recruitment to the liver with Fpr1 being sole receptor for neutrophils to sense Listeria chemoattractant signals and for production of bactericidal superoxide. PMID: 23139859
  • findings may have clinical significance because current smokers and subjects with emphysema showed increased FPR expression in bronchoalveolar fluids and on peripheral neutrophils PMID: 22461430
  • Neutrophil migration into the inflamed mouse colon does not depend on FPR1, but FPR1 contributes in other pathological mechanisms that are harmful during acute inflammation but are protective during chronic inflammation. PMID: 22383080
  • Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3 PMID: 21921027
  • Fpr1 has a role in modulation of anxiety-like behavior and fear memory by regulating glucocorticoid production PMID: 21484271
  • The N-formylpeptide receptor (FPR) and a second G(i)-coupled receptor mediate fMet-Leu-Phe-stimulated activation of NADPH oxidase in murine neutrophils. PMID: 12470609
  • Leukocyte antiadhesive and anti-inflammatory actions of annexin 1 involve this receptor. PMID: 12560218
  • a novel TLR4-linked signaling pathway that selectively couples to the stabilization of FPR1 mRNA. PMID: 17277163
  • The mechanisms through which these two small GTPases Rac1 and Rac2 mediate free barbed ends generation downstream of the formyl-methionyl-leucyl-phenylalanine receptor, was investigated. PMID: 17954607
  • study found that mFPR1 is responsible for the high potency of fMIVIL and fMIFL; the ability of mFPR1 to detect bacterially derived formyl peptides indicates that this important host defense mechanism is conserved in mice PMID: 18606697
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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