|Calculated MW||31836 Da|
|Homology||Mouse- 15/16 amino acid residues identical; human- 12/16 amino acid residues identical.|
|Other Names||Free fatty acid receptor 1, G-protein coupled receptor 40, Ffar1, Gpr40|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide, (C)NVASFINPDLEGSWRK corresponding to amino acid residues 244-259 of rat free fatty acid receptor 1 (Accession Q8K3T4).|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||1 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 DDW.|
|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.
Free fatty acids (FFAs) were for long believed to influence cellular metabolism. Hoever, the discovery that FFAs actually mediate their effects through one of three G-protein coupled receptors (GPCRs) - Free Fatty Acid Receptors 1-3 (FFAR1-3), has initiated a number of studies in order to assess their implication in health and disease1. Like all other GPCRs, FFAR1-3 have seven transmembrane domains, an extracellular N-terminal tail and an intracellular C-terminus. FFAR1 is activated by either medium or long, saturated or unsaturated fatty acids2,3, whereas FFAR2 and FFAR3 are activated by short chain fatty acids4,5. FFAR1 is coupled to Gq and leads to Ca2+ mobilization upon activation. FFAR2 couples to both pertussis-sensitive and insensitive G-proteins and also leads to increased intracellular Ca2+ levels. FFAR3 coupling to G-protein induces an increase in cAMP1. Distribution studies of all three FFA Receptors indicate that FFAR1 mRNA is quite elevated in the pancreas2,3. FFAR1 is also detected in the liver, heart, skeletal muscle, and brain; although this broad localization pattern is supported only by one study2. FFAR2 is expressed in many tissues like liver and colon6. FFAR3 is expressed in many tissues but shows highest expression in adipose tissue4. Relatively high expression of the receptor could be detected in pancreas, spleen, lymph nodes and bone marrow4,5. As mentioned above, the finding that FFAs’ actions are mediated by GPCRs, prompted many studies in order to elucidate their roles in healthy and disease states. Such studies stipulate that FFAR1 may be involved in obesity and type 2 diabetes since circulating free fatty acid levels in the plasma are significantly elevated. On the other hand, FFAR2 and FFAR3 could be potential targets for treating irritable bowel disease and appetite control1. Abgent is pleased to offer a highly specific antibody directed against an epitope of rat FFAR1. Anti-Free Fatty Acid Receptor 1 (extracellular) antibody (#AG1280) can be used in western blot analysis and has been designed to recognize FFAR1 from mouse, rat and human samples.
References 1. Stoddart, L.A. et al. (2008) Pharmacol. Rev. 60, 405. 2. Briscoe, C.P. et al. (2003) J. Biol. Chem. 278, 11303. 3. Itoh, Y. et al. (2003) Nature 422, 173. 4. Brown, A.J. et al. (2003) J. Biol. Chem. 278, 11312. 5. Le Poul, E. et al. (2003) J. Biol. Chem. 278, 25481. 6. Karaki, S. et al. (2006) Cell. Tissue Res. 324, 353.
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