Complement C3 Recombinant Protein | C3 recombinant protein

Recombinant Mouse Complement C3 (C3), partial

Cat. Num. AAA1007121

• Gene Names: C3; ASP; Plp; HSE-MSF; AI255234
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Complement C3; Recombinant Mouse Complement C3 (C3); partial; HSE-MSF; C3 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1321-1663. Partial
• Sequence: SEETKQNEAFSLTAKGKGRGTLSVVAVYHAKLKSKVTCKKFDLRVSIRPAPETAKKPEEAKNTMFLEICTKYLGDVDATMSILDISMMTGFAPDTKDLELLASGVDRYISKYEMNKAFSNKNTLIIYLEKISHTEEDCLTFKVHQYFNVGLIQPGSVKVYSYYNLEESCTRFYHPEKDDGMLSKLCHSEMCRCAEENCFMQQSQEKINLNVRLDKACEPGVDYVYKTELTNIELLDDFDEYTMTIQQVIKSGSDEVQAGQQRKFISHIKCRNALKLQKGKKYLMWGLSSDLWGEKPNTSYIIGKDTWVEHWPEAEECQDQKYQKQCEELGAFTESMVVYGCPN

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for C3 recombinant protein

C3 plays a central role in the activation of the complent system. Its processing by C3 convertase is the central reaction in both classical and alternative complent pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates. Derived from proteolytic degradation of complent C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a choattractant for neutrophils. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. The short isoform has B-cell stimulatory activity. C3-beta-c: Acts as a choattractant for neutrophils in chronic inflammation. Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2.

References

Nucleotide sequence of complementary DNA and derived amino acid sequence of murine complement protein C3.Fey G.H., Lundwall A., Wetsel R.A., Tack B.F., de Bruijn M.H.L., Domdey H.Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:333-344(1984) Structure of murine complement component C3. I. Nucleotide sequence of cloned complementary and genomic DNA coding for the beta chain.Lundwall A., Wetsel R.A., Domdey H., Tack B.F., Fey G.H.J. Biol. Chem. 259:13851-13856(1984) Isolation and analysis of genomic DNA clones encoding the third component of mouse complement.Wiebauer K., Domdey H., Diggelmann H., Fey G.Proc. Natl. Acad. Sci. U.S.A. 79:7077-7081(1982) Common evolutionary origin of alpha 2-macroglobulin and complement components C3 and C4.Sottrup-Jensen L., Stepanik T.M., Kristensen T., Lonblad P.B., Jones C.M., Wierzbicki D.M., Magnusson S., Domdey H., Wetsel R.A., Lundwall A., Tack B.F., Fey G.H.Proc. Natl. Acad. Sci. U.S.A. 82:9-13(1985) Structure and expression of the C3 gene.Fey G., Domdey H., Wiebauer K., Whitehead A.S., Odink K.Springer Semin. Immunopathol. 6:119-147(1983) A paracrine migration-stimulating factor for metastatic tumor cells secreted by mouse hepatic sinusoidal endothelial cells identification as complement component C3b.Hamada J., Cavanaugh P.G., Miki K., Nicolson G.L.Cancer Res. 53:4418-4423(1993) The specific production of the third component of complement by osteoblastic cells treated with 1 alpha,25-dihydroxyvitamin D3.Sato T., Hong M.H., Jin C.H., Ishimi Y., Udagawa N., Shinki T., Abe E., Suda T.FEBS Lett. 285:21-24(1991) Amino acid sequences of mouse complement C3 derived from nucleotide sequences of cloned cDNA.Fey G.H., Wiebauer K., Domdey H.Ann. N. Y. Acad. Sci. 421:307-312(1983) Structure of murine complement component C3. II. Nucleotide sequence of cloned complementary DNA coding for the alpha chain.Wetsel R.A., Lundwall A., Davidson F., Gibson T., Tack B.F., Fey G.H.J. Biol. Chem. 259:13857-13862(1984) Characterization of the mRNA and cloned cDNA specifying the third component of mouse complement.Domdey H., Wiebauer K., Kazmaier M., Mueller V., Odink K., Fey G.H.Proc. Natl. Acad. Sci. U.S.A. 79:7619-7623(1982) The structure of an alternate form of complement C3 that displays costimulatory growth factor activity for B lymphocytes.Cahen-Kramer Y., Martensson I.L., Melchers F.J. Exp. Med. 180:2079-2088(1994) Acylation-stimulating protein (ASP) deficiency induces obesity resistance and increased energy expenditure in ob/ob mice.Xia Z., Sniderman A.D., Cianflone K.J. Biol. Chem. 277:45874-45879(2002) Acylation-stimulating protein deficiency and altered adipose tissue in alternative complement pathway knockout mice.Paglialunga S., Fisette A., Yan Y., Deshaies Y., Brouillette J.F., Pekna M., Cianflone K.Am. J. Physiol. 294:E521-E529(2008)

NCBI and Uniprot Product Information

• NCBI GI #: 126518317
• NCBI GeneID: 12266
• NCBI Accession #: NP_033908.2
• NCBI GenBank Nucleotide #: NM_009778.3
• UniProt Accession #: P01027; Q61370; Q80XP1
• Molecular Weight: 55.3 kDa
• NCBI Official Full Name: complement C3 preproprotein
• NCBI Official Synonym Full Names: complement component 3
• NCBI Official Symbol: C3
• NCBI Official Synonym Symbols: ASP; Plp; HSE-MSF; AI255234
• UniProt Protein Name: Complement C3
• Protein Family: Complement C3
• UniProt Gene Name: C3
• UniProt Synonym Gene Names: C3bc; ASP
• UniProt Entry Name: CO3_MOUSE

NCBI Description

This gene encodes complement protein C3 which plays a central role in the classical, alternative and lectin activation pathways of the complement system. The encoded preproprotein undergoes a multi-step processing to generate various functional peptides. Mice deficient in the encoded protein fail to clear bacteria from the blood stream upon infection, display diminished airway hyperresponsiveness and lung eosinophilia upon allergen-induced pulmonary allergy, and develop severe lung injury after deposition of IgG immune complexes. Deficiency of the homolog of the encoded protein in humans was found to be associated with increased susceptibility to infections, age-related macular degeneration, and atypical hemolytic uremic syndrome. [provided by RefSeq, Mar 2015]

Uniprot Description

C3: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates. Defects in C3 are the cause of complement component 3 deficiency (C3D). A rare defect of the complement classical pathway. Patients develop recurrent, severe, pyogenic infections because of ineffective opsonization of pathogens. Some patients may also develop autoimmune disorders, such as arthralgia and vasculitic rashes, lupus-like syndrome and membranoproliferative glomerulonephritis. Genetic variation in C3 is associated with susceptibility to age-related macular degeneration type 9 (ARMD9). ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin- containing structure known as Bruch membrane. Defects in C3 are a cause of susceptibility to hemolytic uremic syndrome atypical type 5 (AHUS5). An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype. Increased levels of C3 and its cleavage product ASP, are associated with obesity, diabetes and coronary heart disease. Short-term endurance training reduces baseline ASP levels and subsequently fat storage.

Protein type: Inhibitor; Secreted; Secreted, signal peptide

Cellular Component: extracellular region; extracellular space

Molecular Function: C5L2 anaphylatoxin chemotactic receptor binding; cofactor binding; endopeptidase inhibitor activity; lipid binding; protein binding

Biological Process: blood coagulation; complement activation; complement activation, alternative pathway; complement activation, classical pathway; fatty acid metabolic process; immune system process; inflammatory response; innate immune response; lipid metabolic process; positive regulation of activation of membrane attack complex; positive regulation of angiogenesis; positive regulation of developmental growth; positive regulation of G-protein coupled receptor protein signaling pathway; positive regulation of phagocytosis; positive regulation of protein amino acid phosphorylation; positive regulation of type IIa hypersensitivity