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human fpr1 gene (OriGene)

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OriGene human fpr1 gene
Human Fpr1 Gene, supplied by OriGene, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fpr1+gene/FPR1+(NM_002029)+Human+Untagged+Clone/pm40987405-72-5-9
Average 93 stars, based on 4 article reviews

human fpr1 gene - by Bioz Stars, 2026-10

93/100 stars

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Stable Transfection:

Article Title: Propofol inhibits superoxide production, elastase release, and chemotaxis in formyl peptide-activated human neutrophils by blocking formyl peptide receptor 1.
Article Snippet: .. HEK-293 were stably transfected with the pCMV6AC vector containing the human FPR1 gene (NM_002029; OriGene, Rockville, MD) for 72 h using X-tremeGENEHp DNA transfection reagent (Roche, Mannheim, Germany), according to the manufacturer’s instruction. ..

Article Title: Dipeptide HCH6-1 inhibits neutrophil activation and protects against acute lung injury by blocking FPR1.
Article Snippet: Formyl peptide receptor 1 (FPR1) is an emerging therapeutic target for the discovery of drugs to treat neutrophilic inflammatory diseases.. However, development of FPR1 antagonists for clinical use is still inadequate.. The purpose of this study was to identify a synthetic dipeptide N-(N-benzoyl-L-tryptophanyl)-Dphenylanlanine methyl ester (HCH6-1) as a FPR1 inhibitor and to investigate its protective effects against acute lung injury (ALI).

Article Title: Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
Article Snippet: .. HEK-293 were stably transfected with the pCMV6-AC vector containing the human FPR1 gene (NM_002029; OriGene, Rockville, MD) using X-treme GENE Hp DNA transfection reagent (Roche, Mannheim, Germany). ..

Transfection:

Article Title: Butyrolactone I from Aspergillus fungi blocks neutrophil FPR1 to alleviate acute respiratory distress syndrome.
Article Snippet: This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record.. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article.. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

Modification:

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a Overall structures of fMLF–FPR1–G i1 , fM5–FPR2–G i2 , fM9–FPR2–G i2 , fHN–FPR2–G i2 , and Aβ 42 –FPR2–G i2 complexes. The cryo-EM maps and structures are colored according to chains. The peptide ligands are shown as spheres. b Cut-away view of ligand-binding pockets in the peptide agonist–FPR–G i structures. The receptors are shown as surface and cartoon representations. The ligands are shown as sticks. c , d Interactions between the FPRs and the N termini of the peptide agonists. The N-terminal residue fM1 of the peptides in the structures of fMLF–FPR1–G i1 , fM5–FPR2–G i2 , fM9–FPR2–G i2 , and fHN–FPR2–G i2 , and the N-terminal peptide residues D1 and A2 in the Aβ 42 –FPR2–G i2 structure are shown as sticks. The receptor residues that interact with the peptide N termini are also shown as sticks. Only the receptor in the fM5–FPR2–G i2 structure is shown in blue cartoon representation for clarity. c Interactions between the FPRs and the side chains of the peptide N termini. d Interactions between the FPRs and the N -formyl groups at the N termini of the peptides. The N -formyl groups are highlighted by a red dashed circle. e – h Peptide agonist-induced IP accumulation of FPR1 and FPR2 mutants. Bars represent differences in calculated peptide agonist potency (pEC 50 ) for each mutant relative to the wild-type receptor (WT). Data are shown as mean ± SEM (bars) from at least three independent experiments performed in triplicate with individual data points shown (dots). * P < 0.05, ** P < 0.001, *** P < 0.0001 by one-way analysis of variance followed by Dunnett’s post-test compared with the response of the wild-type receptor. Supplementary Table provides detailed statistical evaluation, P -values, numbers of independent experiments ( n ), and expression levels. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Structural basis of FPR2 in recognition of Aβ 42 and neuroprotection by humanin

doi: 10.1038/s41467-022-29361-x

Figure Lengend Snippet: a Overall structures of fMLF–FPR1–G i1 , fM5–FPR2–G i2 , fM9–FPR2–G i2 , fHN–FPR2–G i2 , and Aβ 42 –FPR2–G i2 complexes. The cryo-EM maps and structures are colored according to chains. The peptide ligands are shown as spheres. b Cut-away view of ligand-binding pockets in the peptide agonist–FPR–G i structures. The receptors are shown as surface and cartoon representations. The ligands are shown as sticks. c , d Interactions between the FPRs and the N termini of the peptide agonists. The N-terminal residue fM1 of the peptides in the structures of fMLF–FPR1–G i1 , fM5–FPR2–G i2 , fM9–FPR2–G i2 , and fHN–FPR2–G i2 , and the N-terminal peptide residues D1 and A2 in the Aβ 42 –FPR2–G i2 structure are shown as sticks. The receptor residues that interact with the peptide N termini are also shown as sticks. Only the receptor in the fM5–FPR2–G i2 structure is shown in blue cartoon representation for clarity. c Interactions between the FPRs and the side chains of the peptide N termini. d Interactions between the FPRs and the N -formyl groups at the N termini of the peptides. The N -formyl groups are highlighted by a red dashed circle. e – h Peptide agonist-induced IP accumulation of FPR1 and FPR2 mutants. Bars represent differences in calculated peptide agonist potency (pEC 50 ) for each mutant relative to the wild-type receptor (WT). Data are shown as mean ± SEM (bars) from at least three independent experiments performed in triplicate with individual data points shown (dots). * P < 0.05, ** P < 0.001, *** P < 0.0001 by one-way analysis of variance followed by Dunnett’s post-test compared with the response of the wild-type receptor. Supplementary Table provides detailed statistical evaluation, P -values, numbers of independent experiments ( n ), and expression levels. Source data are provided as a Source Data file.

Article Snippet: The genes of human FPR1 and FPR2 were codon-optimized and synthesized by Sangon Biotech for insect-cell expression.

Techniques: Cryo-EM Sample Prep, Ligand Binding Assay, Residue, Mutagenesis, Expressing

a Binding pocket for Aβ 42 in FPR2. The Aβ 42 –FPR2–G i2 structure is shown in both side (left) and extracellular (right) views. Aβ 42 is shown as sticks and colored magenta (N-terminal part) and pink (C-terminal part). b Inhibition of WK(FITC)YMVm binding to wild-type FPR2 by Aβ 42 , Aβ 40 , or Aβ 1–12 . Data are displayed as mean ± SEM from at least three independent experiments ( n ) performed in triplicate (Aβ 42 , n = 18; Aβ 40 and Aβ 1–12 , n = 3). Source data are provided as a Source Data file. c – e , Interactions between FPR2 and Aβ 42 . Aβ 42 residues and the receptor residues that are involved in interactions are shown as sticks. Polar interactions are shown as red dashed lines. c Interactions between FPR2 and the Aβ 42 residues D1–E3. d Interactions between FPR2 and the Aβ 42 residues E3–R5. e Interactions between FPR2 and the Aβ 42 residues R5–Y10.

Journal: Nature Communications

Article Title: Structural basis of FPR2 in recognition of Aβ 42 and neuroprotection by humanin

doi: 10.1038/s41467-022-29361-x

Figure Lengend Snippet: a Binding pocket for Aβ 42 in FPR2. The Aβ 42 –FPR2–G i2 structure is shown in both side (left) and extracellular (right) views. Aβ 42 is shown as sticks and colored magenta (N-terminal part) and pink (C-terminal part). b Inhibition of WK(FITC)YMVm binding to wild-type FPR2 by Aβ 42 , Aβ 40 , or Aβ 1–12 . Data are displayed as mean ± SEM from at least three independent experiments ( n ) performed in triplicate (Aβ 42 , n = 18; Aβ 40 and Aβ 1–12 , n = 3). Source data are provided as a Source Data file. c – e , Interactions between FPR2 and Aβ 42 . Aβ 42 residues and the receptor residues that are involved in interactions are shown as sticks. Polar interactions are shown as red dashed lines. c Interactions between FPR2 and the Aβ 42 residues D1–E3. d Interactions between FPR2 and the Aβ 42 residues E3–R5. e Interactions between FPR2 and the Aβ 42 residues R5–Y10.

Article Snippet: The genes of human FPR1 and FPR2 were codon-optimized and synthesized by Sangon Biotech for insect-cell expression.

Techniques: Binding Assay, Inhibition

a Comparison of fHN- and Aβ 42 -binding sites in FPR2. The peptides fHN and Aβ 42 are shown as green and magenta sticks, respectively. Only the receptor in the fHN–FPR2–G i2 structure is shown in yellow cartoon representation for clarity. b , d , f Binding and cell-signaling assays of FPR2. Bars represent differences in calculated fHN-binding affinity (p K i ; b , f ) or potency (pEC 50 , d ) for each mutant relative to the wild-type receptor or peptide (WT). Data are displayed as mean ± SEM (bars) from at least three independent experiments performed in triplicate with individual data points shown (dots). * P < 0.05, ** P < 0.001, *** P < 0.0001 by one-way analysis of variance followed by Dunnett’s post-test compared with the response to the wild-type fHN ( b ) or the response of the wild-type receptor ( d , f ). Supplementary Tables , provide detailed statistical evaluation, P -values, numbers of independent experiments ( n ), and expression levels. Source data are provided as a Source Data file. b Inhibition of WK (FITC) YMVm binding to wild-type FPR2 by fHN variants. d fHN-induced IP accumulation of FPR2 mutants. f Inhibition of WK (FITC)YMVm binding to FPR2 mutants by fHN. c , e Interactions between FPR2 and fHN. The fHN residues and the receptor residues involved in interactions are shown as sticks. Polar interactions are shown as red dashed lines. c Interactions between FPR2 and the fHN residues fM1–P3. e Interactions between FPR2 and the fHN residues R4–S14. The two hydrophobic interaction cores are highlighted by two black dashed circles.

Journal: Nature Communications

Article Title: Structural basis of FPR2 in recognition of Aβ 42 and neuroprotection by humanin

doi: 10.1038/s41467-022-29361-x

Figure Lengend Snippet: a Comparison of fHN- and Aβ 42 -binding sites in FPR2. The peptides fHN and Aβ 42 are shown as green and magenta sticks, respectively. Only the receptor in the fHN–FPR2–G i2 structure is shown in yellow cartoon representation for clarity. b , d , f Binding and cell-signaling assays of FPR2. Bars represent differences in calculated fHN-binding affinity (p K i ; b , f ) or potency (pEC 50 , d ) for each mutant relative to the wild-type receptor or peptide (WT). Data are displayed as mean ± SEM (bars) from at least three independent experiments performed in triplicate with individual data points shown (dots). * P < 0.05, ** P < 0.001, *** P < 0.0001 by one-way analysis of variance followed by Dunnett’s post-test compared with the response to the wild-type fHN ( b ) or the response of the wild-type receptor ( d , f ). Supplementary Tables , provide detailed statistical evaluation, P -values, numbers of independent experiments ( n ), and expression levels. Source data are provided as a Source Data file. b Inhibition of WK (FITC) YMVm binding to wild-type FPR2 by fHN variants. d fHN-induced IP accumulation of FPR2 mutants. f Inhibition of WK (FITC)YMVm binding to FPR2 mutants by fHN. c , e Interactions between FPR2 and fHN. The fHN residues and the receptor residues involved in interactions are shown as sticks. Polar interactions are shown as red dashed lines. c Interactions between FPR2 and the fHN residues fM1–P3. e Interactions between FPR2 and the fHN residues R4–S14. The two hydrophobic interaction cores are highlighted by two black dashed circles.

Article Snippet: The genes of human FPR1 and FPR2 were codon-optimized and synthesized by Sangon Biotech for insect-cell expression.

Techniques: Comparison, Binding Assay, Mutagenesis, Expressing, Inhibition

a – c Interactions between FPR2 and the formyl peptides. Only the receptor in the fM5–FPR2–G i2 ( a , b ) or fM9–FPR2–G i2 structure ( c ) is shown in cartoon representation for clarity. a Interactions between FPR2 and the residues Y/L2 and I4 in fM5 and fM9. b Interactions between FPR2 and the residues F3 and I5/I6 in fM5 and fM9. c Interactions between FPR2 and the residues N5 and L7 in fM9. Polar interactions are shown as red dashed lines. d Interactions between FPR1 and the residues L2 and F3 in fMLF. The peptide fM5 and FPR2 residues L81 2.60 and F257 6.51 in the fM5–FPR2–G i2 structure are also shown for comparison. The red arrow indicates the movement of fMLF relative to fM5. e , f Surfaces of the FPRs are colored according to their electrostatic potential from red (negative) to blue (positive), showing different charge distributions at the entrance to the ligand-binding pocket in the two receptors. e The peptide fMLF and the receptor residues R84 2.63 , K85 2.64 , G89, and G280 7.32 in the fMLF–FPR1–G i1 structure are shown as sticks. f The receptor residues S84 2.63 , M85 2.64 , E89, and D281 7.32 in the fM9–FPR2–G i2 structure are shown as sticks. The peptide fMLF in the fMLF–FPR1–G i1 structure is also shown. The green “x” indicates that the negatively charged C terminus of fMLF repels the acidic residues E89 and D281 7.32 in FPR2.

Journal: Nature Communications

Article Title: Structural basis of FPR2 in recognition of Aβ 42 and neuroprotection by humanin

doi: 10.1038/s41467-022-29361-x

Figure Lengend Snippet: a – c Interactions between FPR2 and the formyl peptides. Only the receptor in the fM5–FPR2–G i2 ( a , b ) or fM9–FPR2–G i2 structure ( c ) is shown in cartoon representation for clarity. a Interactions between FPR2 and the residues Y/L2 and I4 in fM5 and fM9. b Interactions between FPR2 and the residues F3 and I5/I6 in fM5 and fM9. c Interactions between FPR2 and the residues N5 and L7 in fM9. Polar interactions are shown as red dashed lines. d Interactions between FPR1 and the residues L2 and F3 in fMLF. The peptide fM5 and FPR2 residues L81 2.60 and F257 6.51 in the fM5–FPR2–G i2 structure are also shown for comparison. The red arrow indicates the movement of fMLF relative to fM5. e , f Surfaces of the FPRs are colored according to their electrostatic potential from red (negative) to blue (positive), showing different charge distributions at the entrance to the ligand-binding pocket in the two receptors. e The peptide fMLF and the receptor residues R84 2.63 , K85 2.64 , G89, and G280 7.32 in the fMLF–FPR1–G i1 structure are shown as sticks. f The receptor residues S84 2.63 , M85 2.64 , E89, and D281 7.32 in the fM9–FPR2–G i2 structure are shown as sticks. The peptide fMLF in the fMLF–FPR1–G i1 structure is also shown. The green “x” indicates that the negatively charged C terminus of fMLF repels the acidic residues E89 and D281 7.32 in FPR2.

Article Snippet: The genes of human FPR1 and FPR2 were codon-optimized and synthesized by Sangon Biotech for insect-cell expression.

Techniques: Comparison, Ligand Binding Assay

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