Recombinant Mouse Complement Component C3a Protein, CF

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
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Recombinant Mouse Complement Component C3a Protein, CF Summary

Details of Functionality
Measured by its ability to enhance IL-6 secretion by human peripheral blood mononuclear cells (PBMC). Fischer, W.H. et al. (1999) J. Immunol. 162:453. The ED50 for this effect is typically 0.8-4 µg/mL
Source
E. coli-derived mouse Complement Component C3a protein
Ser671-Arg748
Accession #
N-terminal Sequence
Ser671
Protein/Peptide Type
Recombinant Proteins
Gene
C3
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
9.2 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
9 kDa, reducing conditions
Publications
Read Publications using
8085-C3 in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Complement Component C3a Protein, CF

  • AHUS5;ARMD9;ASP;C3a;C3b;Complement C3;CPAMD1;HEL-S-62p
  • Anaphylatoxin
  • C3
  • Complement Component C3a

Background

C3a is an anaphylotoxin polypeptide comprising amino acids (aa) 671-748 of the Complement C3 precursor protein (1-4). Anaphylatoxins are proteolytically generated from the C3, C4 and C5 alpha chains by convertases formed by other complement fragments (2). They share 30-36% aa identity, and mediate inflammatory responses that vary in strength in the order C5a > C3a > C4a (2). Like C4a and C5a, the 78 aa, 9 kDa mouse C3a contains six conserved cysteine residues that form a knot structure and possess an overall basic charge (4, 5). It is not glycosylated (4). The C-terminal regions of C3a and C4a show antimicrobial activity, while C5a is chemotactic but not antimicrobial (5). Mouse C3a shares 94% aa sequence identity with rat, and 65-69% with human, guinea pig, bovine, porcine and canine C3a. C3a formation is common to all three pathways of complement activation: classical (antibody-mediated), lectin and alternative (1, 2). It binds the G-protein coupled C3a receptor (C3aR) on myeloid peripheral blood leukocytes, and on activated lymphocytes, endothelial and internal organ epithelial cells (6, 7). C3a contributes to both innate and adaptive immunity. It activates mast cells and neutrophils, triggering robust mast cell degranulation in airways during asthmatic allergen challenges (8). It enhances lipopolysaccharide-induced prostaglandin, cytokine and chemokine secretion by macrophages and other cells (1, 6, 9, 10). It assists in Th2-type inflammatory reactions, promotes Th1 cell maturation, and down-regulates regulatory T cell differentiation (8, 11). It stimulates leukocyte chemotaxis and smooth muscle contraction (8, 9).  Endogenous carboxypeptidase-N can remove the arginine at the C-terminus of the anaphylatoxins to create desArg forms (1). C3adesArg, also called ASP (Acylation-Stimulating Protein) is an adipocyte-derived protein that binds the C5L2 receptor (GPR77) and stimulates adipose tissue triglyceride synthesis (2, 7, 12). The anaphylactic activity of ASP is weaker than that of C3a (7, 10). C5L2 is also involved in C3a and C5a activity (12).
  1. Markiewski, M. and J.D. Lambris (2007) Am. J. Pathol. 171:715.
  2. Haas, P-J. and J. van Strijp (2007) Immunol. Res. 37:161.
  3. Domdey, H. et al. (1982) Proc. Natl. Acad. Sci. USA 79:7619.
  4. Hugli, T.E. (1975) J. Biol. Chem. 250:8293.
  5. Pasupuleti, M. et al. (2007) J. Biol. Chem. 282:2520.
  6. Thurman, J.M. et al. (2007) J. Immunol. 178:1819.
  7. Kalant, D. et al. (2005) J. Biol. Chem. 280:23936.
  8. Ali, H. and R.A. Panettieri (2005) Respir. Res. 6:19.
  9. Honczarenko, M. et al. (2005) J. Immunol. 175:3698.
  10. Fischer, W.H. et al. (1999) J. Immunol. 162:453.
  11. van der Touw, W. et al. (2013) J. Immunol. 190:5921.
  12. Chen, N-J. et al. (2007) Nature 446:203.

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Bioinformatics

Gene Symbol C3
Uniprot