rabbit polyclonal anti c5ar antibody (Novus Biologicals)
Novus Biologicals is a verified supplier 
Novus Biologicals manufactures this product 
86
Structured Review
Novus Biologicals
rabbit polyclonal anti c5ar antibody
Rabbit Polyclonal Anti C5ar Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+polyclonal+anti+c5ar+antibody/10__1074_slash_jbc__m110__129213-77-40-49?v=Novus+Biologicals
Average 86 stars, based on 1 article reviews
Rabbit Polyclonal Anti C5ar Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+polyclonal+anti+c5ar+antibody/10__1074_slash_jbc__m110__129213-77-40-49?v=Novus+Biologicals
Average 86 stars, based on 1 article reviews
rabbit polyclonal anti c5ar antibody - by Bioz Stars,
2026-08
86/100 stars
Images
1) Product Images from "Third Extracellular Loop (EC3)-N Terminus Interaction Is Important for Seven-transmembrane Domain Receptor Function"
Article Title: Third Extracellular Loop (EC3)-N Terminus Interaction Is Important for Seven-transmembrane Domain Receptor Function
Journal: Journal of Biological Chemistry
doi: 10.1074/jbc.m110.129213
Figure Legend Snippet: FIGURE 1. Sequence alignment of CXCR4 and C5aR with rhodopsin highlighting the most conserved residues and the known activation switches in GPCRs. Ballesteros and Weinstein nomenclature assigns X.50, to the “fingerprint residues” shown as white letters with black background in each transmembrane domain. Important transmembrane activation domains are shaded in gray. Conserved cysteine residues par- ticipatingindisulfidebondformationareshownwithgrayboxes.Residuesshownwithblackboxesindicatelack of complementary charged residues at 6.30 to support the ionic lock activation switch. Point mutation known to confer constitutive activity in CXCR4 is shown with white box. Residues shown as underlined have been subjected to mutagenesis for engineering C5aR. Residues marked with stars have been mutated to cysteine in other studies for engineering an extra disulfide bond between EC3 and N terminus of rhodopsin.
Techniques Used: Sequencing, Activation Assay, Mutagenesis, Activity Assay
Figure Legend Snippet: FIGURE 3. Engineering C5aR to a chemokine-type receptor; signaling profile of mutant C5aR receptors, co-expressed with C5a in yeast. Left panel, canonical receptor topology for C5aR. The N119S mutation on TM3isanovelconstitutivelyactivemutantidentifiedforC5aRinthisstudy.Asp27,Ser30,andSer272,highlighted in white with black background, have been mutated to cysteine for engineering a possible extra disulfide linkage between the N terminus and EC3 loop of C5aR. Middle and right panel, respectively, illustrate the effect of S30C, S272C, S30C/S272C, and D27C, S272C, D27C/S272C on C5a-stimulated C5aR signaling. Vector repre- sents the -galactosidase activity of the engineered yeast in the absence of both receptor and ligand. Each bar represents means S.D. of signaling activity for three independent transformants, and data are representative of at least two independent experiments.
Techniques Used: Mutagenesis, Plasmid Preparation, Activity Assay
Figure Legend Snippet: FIGURE 4. Signaling profile of wild type and mutant C5aR receptors, co- expressed with wild type and C27R C5a in yeast. The nonfunctional mutants, such as S272A and S272T, have not been tested with C27R C5a. Vector represents the -galactosidase activity of the engineered yeast in the absence of both receptor and ligand. Each bar represents means S.D. of signaling activity for three independent transformants, and data are repre- sentative of at least two independent experiments.
Techniques Used: Mutagenesis, Plasmid Preparation, Activity Assay
Figure Legend Snippet: FIGURE 5. Effect of point mutations on expression profile of C5aR in yeast as assessed by Western blot. 25 l of whole yeast lysates expressing the mutant or the wild type receptors were resolved on a 4–12% BisTris gel and detected as described under “Experimental Procedures.” The single and dou- ble asterisks, respectively, indicate the full-length and proteolytic fragments of the receptors. n/a, not applicable.
Techniques Used: Expressing, Western Blot, Mutagenesis
Figure Legend Snippet: FIGURE 6. Comparison of signaling profile of wild type, D282A, and S272A mutant C5aR receptors, co-expressed with C5a and metabolite C5a-des-Arg74 in yeast. C5a-des-Arg74 stimulates only 30% of the signal- ing in wild type C5aR compared with the signaling stimulated in response to C5a. D282A mutant displays reduced signaling in response to C5a consistent with other studies but displays near-maximal signaling in response to metab- olite C5a-des-Arg74. The nonfunctional mutant S272A neither responds to C5a nor to the metabolite C5a-des-Arg74. Vector represents the -galactosid- ase activity of the engineered yeast in the absence of both receptor and ligand. Each bar represents means S.D. of signaling activity for three inde- pendent transformants, and data are representative of at least two indepen- dent experiments.
Techniques Used: Comparison, Mutagenesis, Plasmid Preparation, Activity Assay
Figure Legend Snippet: FIGURE 8. Positional effect of N-terminal and EC3 cysteines on constitu- tive signaling profile of C5aR and their respective response to C5a, co- expressed in yeast. Left and right panels, respectively, illustrate the effect of S30C, S272C, S30C/S272C, and D27C, S272C, D27C/S272C on ligand-indepen- dent and -dependent signaling of constitutively active C5aR. The contrasting effect of S30C/S272C, D27C/S272C, and S272C on constitutive signaling of C5aR is noted in both panels. Vector represents the -galactosidase activity of the engineered yeast in the absence of both receptor and ligand. Each bar represents means S.D. of signaling activity for three independent transfor- mants, and data are representative of at least two independent experiments.
Techniques Used: Plasmid Preparation, Activity Assay
Figure Legend Snippet: FIGURE 9. Probing the side chain effect at Ser272 of EC3 on constitutive signaling of C5aR in yeast. The constitutive signaling profile of S272T, S272A, and S272C mutants in the presence and absence of S30C at the N terminus of C5aR. Maximal signaling is noted for all the single and double mutants in response to C5a. Vector represents the -galactosidase activity of the engineered yeast in the absence of both receptor and ligand. Each bar represents means S.D. of signaling activity for three independent transfor- mants, and data are representative of at least two independent experiments.
Techniques Used: Plasmid Preparation, Activity Assay
Figure Legend Snippet: FIGURE10.SignalingassaysinCOS-7cellsexpressingG16withwildtype or mutant receptors. Left and right panels, respectively, represent C5aR and CXCR4. The cells were stimulated with 10 nM C5a (C5aR) or 100 nM CXCL12 (CXCR4). IP3 accumulation values are normalized to the mock transfections, where each bar represents means S.D. of three independent experiments.
Techniques Used: Mutagenesis, Transfection
Figure Legend Snippet: FIGURE 11. Hypothetical molecular models of C5aR and illustration of conformational changes in EC3 due to disulfide linkage and receptor activation. Molecular models of wild type and engineered C5aR are pre- sented, respectively, in A and B. Asp27, Ser30, Asn119, and Ser272 that have been mutated for engineering the C5aR are highlighted in spheres. B, highlight of both the conserved and the engineered disulfide bond, respectively, between Cys109–Cys188 and Cys30–Cys272 in spheres, in con- text of other residues. Loop structures have been smoothed for clarity. C, structural alignment of EC3 of wild type (green loop with cyan helices, 1F88) and engineered rhodopsin (magenta loop with sand helices, Protein Data Bank code 2J4Y). Disulfide linkage between Asp282 of EC3 with Asn2 of the N terminus increases the EC3 loop length by straightening the TM7 by one helical loop. D, structural alignment of EC3 of rhodopsin (green loop with cyan helices, Protein Data Bank code 1F88) with EC3 of appar- ently active opsin (red loop with lime helices, Protein Data Bank code 3DQB). Major conformational changes noted in EC3 are associated with straightening of both TM6 and TM7 helices.
Techniques Used: Activation Assay
