|Application ||FC, WB|
|Calculated MW||38446 Da|
|Homology||Human only. Not recommended for use with rat and mouse samples.|
|Other Names||fMet-Leu-Phe receptor, fMLP receptor, N-formyl peptide receptor, FPR, N-formylpeptide chemoattractant receptor, FPR1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)NFSPWTNDPKERIN, corresponding to amino acid residues 179-192 of human FPR1 (Accession P21462). 2nd extracellular loop.|
|Peptide Confirmation||Confirmed by amino acid analysis and by mass-spectrography.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||Add 50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Chemotactic factors from both Gram-positive and Gram-negative bacteria are short peptides with N-formyl methionine at the N-terminus (extensively reviewed in reference 1). These peptides are released from bacteria during infection and activate formyl peptide receptor (FPR), a member of G-protein coupled receptors (GPCRs). In humans, the FPR family consists mainly of three receptors, FPR1, FPR2/ALX (formerly FPRL1), and FPR3 (formerly FPRL2) which all couple to the Gi subtype of G-proteins and ultimately lead to the activation of phospholipase C and intracellular Ca2+ increase1,2. FPRL1 or FPR2/ALX as commonly called is a seven transmembrane protein like all GPCRs. This receptor was originally cloned by screening a HL60 neutrophil cDNA library with a FPR1 cDNA probe3. FPR2/ALX shares 69% identity with FPR1 and despite its high homology, it displays relatively low affinity for fmlf, the most potent N-formyl peptide released by bacteria3. FPR1 was originally found in neutrophils and later found to be distributed in myeloid and non-myeloid cells as is the case for FPR2/ALX and FPR3 (FPR3 though is not expressed in neutrophils). FPR1 is also expressed in multiple organs and tissues including epithelial cells in organs with secretory functions, endocrine cells, liver hepathocytes, smooth muscle cells and endothelial cells, brain spinal cord and both motor and sensory neurons4. FPR2/ALX has a similar tissue distribution to that of FPR1. While N-formyl peptides were the first peptides found to activate these receptors, the ligand diversity for FPR has proven to be quite broad and demonstrates to be both pro- and anti-inflammatory. They include peptidic ligands originating from bacterial and viral sources (including HIV), endogenous ligands such as chemokines and annexins, short peptides associated with inflammation and infection. Indeed, peptides from Herpes, Ebola and coronavirus 229E are ligands of FPR11. Abgent is pleased to offer a highly specific antibody directed against an extracellular epitope of human FPR1. Anti-Human FPR1 (extracellular) antibody (#AG1282) can be used in western blot analysis and indirect flow cytometry applications. It has been designed to recognize FPR1 from human samples only.
1. Ye, R.D. et al. (2009) Pharmacol. Rev. 61, 119.
2. Le, Y. et al. (2002) Trends Immunol. 23, 541.
3. Murphy, P.M. et al. (1992) J. Biol. Chem. 267, 7637.
4. Becker, E.L. (1998) Cell Tissue Res. 292, 129.
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