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

Name: Recombinant Human Fmet-Leu-Phe Receptor (FPR1) Protein (His-GST&Myc)
Brand: Beta LifeScience
SKU: BLC-02088P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) FPR1.

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Product Overview

Description	Recombinant Human 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	P21462
Target Symbol	FPR1
Synonyms	FPR1; fMet-Leu-Phe receptor; fMLP receptor; N-formyl peptide receptor; FPR; N-formylpeptide chemoattractant receptor
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-GST&C-Myc
Target Protein Sequence	QDFRERLIHALPASLERALTEDSTQTSDTATNSTLPSAEVELQAK
Expression Range	306-350aa
Protein Length	Partial
Mol. Weight	34.9 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	HGNC: 3826 OMIM: 136537 KEGG: hsa:2357 STRING: 9606.ENSP00000302707 UniGene: PMID: 29932988 FPR1 mRNA levels in whole blood can predict the presence of lung cancer. Using this as a reflex test for positive lung cancer screening computed tomography scans has the potential to increase the positive predictive value. PMID: 29313979 To develop enzyme-resistant analogues, we applied here the Retro-Inverso (RI) approach, whereby the topology of the side chains is maintained by inverting the sequence of the peptide and the chirality of all residues. Molecular dynamics suggests that peptide RI-3 adopts the turn structure typical of uPAR-FPR1 antagonists PMID: 28465589 Authors found that the co-expression of uPAR and FPR1 confers to A375 and M14 melanoma cells a clear-cut capability to move towards chemotactic gradients, to cross extracellular matrix and endothelial monolayers. FPR1 activity is required, as cell migration and invasion were abrogated by receptor desensitization. PMID: 29216889 Taken together, our results suggest that intracellular FPR in naive CD4 T cells and surface FPRs in activated CD4 T cells might regulate immune responses by regulating CD4 T cell activity. PMID: 29427663 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 The data demonstrate that FPR1 is involved in neuroblastoma development and could represent a therapy option for the treatment of neuroblastoma. PMID: 27432059 FAM3D plays a role in gastrointestinal homeostasis and inflammation through its receptors FPR1 and FPR2. PMID: 26966188 Formylated MHC class Ib binding peptides activate both human and mouse neutrophils primarily through FPR1. PMID: 27907124 The inhibitory function of oxidant sensing by TRPM2 requires the oxidation of Cys549, which then induces TRMP2 binding to formyl peptide receptor 1 (FPR1) and subsequent FPR1 internalization and signaling inhibition PMID: 27569419 FPR1 expression is significantly upregulated in human masticatory mucosa during wound healing PMID: 28005267 FAM19A4 is a novel ligand of formyl peptide receptor 1. PMID: 25109685 The authors describe here the activation of isolated human blood neutrophils by TcdB and, moreover, by toxin fragments generated by limited proteolytical digestion via the FPR1 receptor. PMID: 25529763 these results highlight the importance of FPR1 in chemotherapy-induced anticancer immune responses. PMID: 26516201 Data suggest that formyl peptide receptor 1 (FPR1) stimulation may represent a novel therapeutic approach to counteract tumor angiogenesis. PMID: 25263443 a pepducin designed to target FPR1 was found to hijack FPR2 and potently inhibit neutrophil functions PMID: 26071379 the co-upregulated expression of mast cell chymase and ANXA1-FPR1 system in ectopic endometrium suggests their involvement in the development of endometriotic lesions. PMID: 25201101 FPR1 rs78488639 interacted with CFH rs800292, HTRA1 rs11200638, and smoking, enhancing risk to exudative age-related macular degeneration and polypoidal choroidal vasculopathy . PMID: 25277308 These results demonstrate that a necroptosis pathway, likely mediated by annexin 1 acting through the FPR1 receptor, contributes to Stevens-Johnson syndrome (SJS) and toxic epidermal necrolysis. PMID: 25031270 A low FPR1/beta1 integrin co-localization was observed. PMID: 24466048 cross-desensitization of CCR1 by FPR1 was associated with CCR1 phosphorylation and moderate reduction of CCR1 cell-surface expression. In contrast, CCR2 was not phosphorylated or internalized after FPR1 activation. PMID: 24778447 FPR1 expression may be used as a novel indicator to predict outcome in gastric cancer patients after gastrectomy. PMID: 24778024 Identification of C-terminal phosphorylation sites of N-formyl peptide receptor-1 (FPR1) in human blood neutrophils. PMID: 23873933 The active F2Pal10 pepducin also triggered a response in cells expressing a mutated FPR2 with the third intracellular loop identical to that of FPR1. PMID: 23562731 Our findings reveal that FPR and FPRL1 are overexpressed in primary melanoma and correlate with aggressive tumor characteristics PMID: 23147350 UPAR, whose expression is regulated by uPA, can, in turn, regulate uPA expression through a mechanism involving its functional interaction with integrins and fMLF-Rs. PMID: 23238745 haplotypic variation in FPR1, especially the SNP p.V101L, alters the receptor's response to cyclosporins PMID: 23373827 The expression of the formyl peptide receptor 1 (FPR1) gene in primary human macrophages is regulated by cytokines and bacterial ligands. PMID: 23185575 FPR1 is functionally expressed on human lens epithelial cells. PMID: 23012360 physiological shear forces alter neutrophil activation via FP PMID: 22768936 analysis of pyrazoles as novel FPR1 antagonists PMID: 22094028 The expression of FPR1 in myeloid cells is developmentally regulated, and the differentiated cells are equipped for immediate response to microbial infections. PMID: 22174875 When normotensive individuals were compared to hypertensives ones, similar FPR1 C32T genotypes and allele frequency distributions were found PMID: 21144844 Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3 PMID: 21921027 Using the homology modeling of the receptors and the ligand docking simulation, here we show that these calpain inhibitors could bind to the putative N-formyl-Met-Leu-Phe (fMLF) binding site on FPR and/or FPRL1. PMID: 22005393 fMLP promotes osteoblast differentiation via the N-formyl peptide receptor 1-mediated signaling pathway in human mesenchymal stem cells from bone marrow PMID: 21372136 This study identifies annexin A1 as part of the anti-inflammatory pattern of apoptotic cells and links the activation of FPRs to established signalling pathways triggering anti-inflammatory responses. PMID: 21254404 This is the first study to evaluate polymorphisms of the FPR1 gene in stomach cancer to find a positive association between these polymorphisms and stomach cancer. PMID: 21216225 These observations suggest a novel signaling role for ANXA1 in mitogen-activated proliferation of breast tumor epithelial cells that is mediated via activation of FPR1 and FPR2. PMID: 20930115 The presence of the C(+) genotype/allele C of FPR301 together with smoking conferred a higher risk for aggressive periodontitis. PMID: 20019777 The expression of FPR is responsible for increased motility of human glioblastoma cells and their formation of highly invasive tumours. PMID: 20197768 A conformational study of human fMLP PMID: 11860029 investigated the direct effect of LXA4 as well as the effect on agonist-induced biological responses using transfected HL-60 cells expressing FPR, FPRL1 or FPRL2 PMID: 12410796 phosphorylation domains differentially regulate arrestin and agonist affinity PMID: 12424254 Critical role of N-terminal N-glycosylation for proper folding of the formyl peptide receptor. PMID: 12565836 Six single nucleotide polymorphisms have been identified including two located in the FPR1 second extracellular loop that are significantly associated with the periodontitis phenotype in African-American patients. PMID: 12595898 Expression of FPRs on transformed or normal fibroblasts indicates that they are able to induce intracellular signaling events leading to fibroblast motility. PMID: 12902510 an annexin 1 peptide can activate FPR, FPRL1, and FPRL2; results indicate that annexin 1 participates in regulating leukocyte emigration into inflamed tissue by activating and desensitizing different receptors of the FPR family. PMID: 15187149 FPR-F110S displayed a delayed and significantly reduced ERK phosphorylation whereas FPR-FSCW nearly lost the ability to phosphorylate ERK PMID: 15195697 FPR and FPRL1, use distinct signaling pathways in activation of human neutrophils PMID: 15625007

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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.

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

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

Product Overview

Target Details

FAQs