Native Human Complement C3c

• Cat.No.: C3-012H

Specification

• Description: C3c is derived from iC3b (inactivated C3b) by proteolytic cleavage (Law, S.K.A. and Reid, K.B.M. (1995)). iC3b is created by cleavage of C3b by factor I in the presence of factor H, CR1 or MCP. C3c can be produced by an additional cleavage by factor I if the iC3b is bound to CR1. Factor H cannot serve as a cofactor for this cleavage. C3c can also be produced by the action of trypsin-like proteases on iC3b. If the C3b precursor was attached to a surface, then the iC3b will remain attached to that surface and when iC3b is cleaved the C3c is released into the surrounding solution while the C3dg/C3d fragment remains on that surface. The breakdown of fluid phase C3b is similar, but in this case both C3c and C3dg/C3d are soluble fragments.Molecular weight: 139,000 daltons composed of three disulfide linked chains
  (75,000 Da, 39,000 Da and 25,000 Da). C3c is glycosylated. There can be considerable
  heterogeneity in the structure of C3c due the fact that it is formed by the action of
  proteases and it is extremely sensitive to additional proteolytic digestion. The initial
  stage of digestion of iC3b (75,000, 63,000, and 39,000 Da) produces C3c (75,000,
  25,000, and 39,000 Da) and C3dg (38,900 Da). The 25,000 Da fragment is from the Nterminal and the 39,000 Da fragment is from the C-terminal of the alpha chain of C3b.
  An additional cleavage of C3dg produces C3d (33,800 Da). The two smaller fragments
  of C3c (25,000, and 39,000 Da) are linked to each other by a disulfide bond and the
  smaller fragment (25,000 Da) is linked to the beta chain (75,000 Da) by a disulfide bond
  (Morley, B.J. and Walport, M.J. (2000); Law, S.K.A. and Reid, K.B.M. (1995); Dodds,
  A.W. and Sim, R.B. editors (1997); Morgan, B.P. ed. (2000)). Some of the chains have a
  C-terminal arginine residue which may be partially cleaved by serum carboxypeptidases
  leading to additional heterogeneity
• Source: Human serum
• Species: Human
• Form: Frozen liquid. None, 0.22 µm filtered.
• Molecular Mass: 139 kDa (3 chains)
• Purity: >90% by SDS-PAGE
• Notes: Use normal precautions for handling human blood products.
• Storage: -70o C or below. Avoid freeze/thaw
• Concentration: 1.0 mg/mL
• Storage Buffer: 10 mM Sodium phosphate, 145 mM NaCl, pH 7.2
• Warning: The source of this protein is human serum, therefore precautions appropriate for handling any blood-derived product must be used even though the source was shown by certified tests to be negative for HBsAg, HTLV-I/II, STS, and for antibodies to HCV, HIV-1 and HIV-II. MSDS sheet is available upon request

Gene Information

• Gene Name: C3 complement component 3 [ Homo sapiens ]
• Official Symbol: C3
• Synonyms: C3; complement component 3; complement C3; CPAMD1; complement component C3; acylation-stimulating protein cleavage product; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1; ASP; AHUS5; ARMD9
• Gene ID: 718
• mRNA Refseq: NM_000064
• Protein Refseq: NP_000055
• MIM: 120700
• UniProt ID: P01024

Reviews

02/23/2022

Expression efficiency is high. In our experiments, we found that the target protein can be synthesized quickly and effectively.

01/26/2022

Activity was not significantly different from the native protein, as expected.

03/23/2021

High purity, no obvious impurities.

Q&As

Have proteins been found to interact with C3 proteins?

Yes, a variety of proteins that interact with C3 proteins, including complement receptors, regulatory proteins, inflammatory factors, etc., have been discovered, and they are jointly involved in the regulation and functional execution of C3 proteins.

What is the relationship between C3 protein and infectious diseases?

C3 protein plays an important role in infectious diseases. It can play an anti-infection role by activating the complement system, directly killing pathogens or enhancing the ability of immune cells to destroy pathogens.

How is the research progress of C3 protein at present?

Research on C3 protein is going on. At present, it mainly focuses on the analysis of its function and regulatory mechanism, the identification of gene mutations associated with diseases, and the interaction with other complement proteins and immune cells, which provides a theoretical basis for the further development of diagnosis and treatment methods of related diseases.

What is the use of C3 protein in laboratory diagnostics?

C3 protein can be used as an aid in the diagnosis of certain immune-related diseases. Measuring the level of C3 protein in serum can reflect the activity of the immune system and the degree of inflammation.

What are the effects of post-translational modifications of C3 protein on its function?

Post-translational modifications of the C3 protein can affect its function. Phosphorylation, cleavage, methylation and other modifications can regulate the activity, stability and interaction ability of C3 proteins.

Have any drug treatments associated with C3 protein been identified?

Yes, some C3 protein-related drug treatments are under development, including drugs that regulate the degree of C3 protein activation, drugs that inhibit the overactivation of C3 protein, etc.