Native Human Complement C3c

• Cat.No.: C3-194H

Specification

• Description: Complement C3 (C3) is the most abundant component of the complement system, with levels in human plasma of ~1.2-1.5 mg/ml. It is central to the activation of both the classical and alternative complement pathways, both of which lead to the proteolytic processing of C3 to C3a and C3b. C3 exists as a heterodimer with molecular masses of 115 kDa and 75 kDa, although it is readily processed to smaller fragments (C3a, C3b, C3c) as evidenced by the molecular weight description below. The current protocol yields C3c, however intact C3 and/or partially processed C3a/C3b may potentially be purified if certain precautions are taken during processing (ie, processing at 4°C, protease inhibitors throughout processing).
• Source: Human Plasma
• Species: Human
• Form: Frozen
• Bio-activity: Not biologically active
• Molecular Mass: 138000
• Purity: >=95% by SDS-PAGE Reacts to C3 antisera on Western Blot Negative against C4 antisera on Western Blot
• Usage: For research use or for use in further manufacturing.
• Quality Control Test: Shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
• Stability: >1 year
• Storage: <= -70°c - avoid>
• Storage Buffer: Phosphate Buffered Saline, pH 7.4
• Tag: Non

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
• Chromosome Location: 19p13.3-p13.2
• Pathway: Activation of C3 and C5, organism-specific biosystem; Adaptive Immune System, organism-specific biosystem; Alternative complement activation, organism-specific biosystem; Chagas disease (American trypanosomiasis), organism-specific biosystem; Chagas disease (American trypanosomiasis), conserved biosystem; Class A/1 (Rhodopsin-like receptors), organism-specific biosystem; Complement Activation, Classical Pathway, organism-specific biosystem
• Function: endopeptidase inhibitor activity; protein binding; receptor binding

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.