|Application ||FC, WB|
|Calculated MW||39336 Da|
|Homology||Human only. Not recommended for use with rat and mouse samples.|
|Other Names||C5a anaphylatoxin chemotactic receptor 1, C5a anaphylatoxin chemotactic receptor, C5a-R, C5aR, CD88, C5AR1, C5AR, C5R1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)DKDTLDLNTPVDK, corresponding to amino acid residues 16-28 of human C5aR (Accession P21730 ). Extracellular, N-terminus.|
|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.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
The innate immune system identifies pathogens by recognizing known elements. This response ultimately leads to the production of proinflammatory substances and the activation of phagocytic neutrophils and macrophages1. Activation of the complement system is an important initial even in the response against pathogens. This system includes some thirty different proteins that act together to form a complex1. C5a is one of the most potent inflammatory peptides generated by complement activation. This peptide has many functions such as acting as a chemoattractant for neutrophils2,3. C5a acts as a vasodilator3,4 and activates the coagulation pathway3,5 just to name a few. C5a exerts its numerous actions by binding to C5aR and C5L2. C5aR belongs to the superfamily of G-protein coupled receptors (GPCRs). Like all members, C5aR has seven transmembrane domains, an extracellular N-terminus and an intracellular C-terminal tail. C5aR can form homodimers6-8 or heteromer with CCR5, chemokine receptor, for example8,9. Activation of C5aR by C5a binding causes Ca2+ mobilization10. C5aR expression is detected in neutrophils, eisinophils, basophils and monocytes3,11,12. The receptor is also expressed in lung and liver13,14. Blocking C5aR by peptides or organic small molecules is in the pipeline for treating chronic inflammatory disorders/diseases like arthritis, inflammatory bowel disease and lung/liver injuries8. Abgent is pleased to offer a highly specific antibody directed against an extracellular epitope of human C5aR. Anti-C5a Anaphylatoxin Receptor (extracellular) antibody (#AG1372) can be used in western blot and indirect flow cytometry applications. It has been designed to recognize C5aR from human samples.
1. Haas, P.J. and van Srijp, J. (2007) Immun. Res. 37, 161.
2. Marder, S.R. et al. (1985) J. Immunol. 134, 3325.
3. Guo, R.F. and Ward, P.A. (2005) Annu. Rev. Immunol. 23, 821.
4. Schumacher, W.A. et al. (1991) Agents Actions 34, 345.
5. Laudes, I.J. et al. (2002) Am. J. Pathol. 160, 1867.
6. Geva, A. et al. (2000) J. Biol. Chem. 275, 35393.
7. Klco, J.M. et al. (2003) J. Biol. Chem. 278, 35345.
8. Monk, P.N. et al. (2007) Br. J. Pharmacol. 152, 429.
9. Huttenrauch, F. et al. (2005) J. Biol. Chem. 280, 37503.
10. Ward, P.A. (2009) J. Mol. Med. 87, 375.
11. Gerard, N.P. et al. (1989) J. Biol. Chem. 264, 1760.
12. Werfel, T. et al. (1992) Blood 79, 152.
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