Native Human C2 Protein

Cat.No.: C2-98H
Description: C2 is central to the activation of both the classical and the lectin pathways of complement. It forms the proteolytic subunit of the C3 and C5 convertase of both pathways. Initiation of each pathway generates proteolytic enzyme complexes which are bound to the target surface (C1q/C1r/C1s in the classical pathway and MBL/ Ficolin/ MASPs in the lectin pathway). C1s and MASP in these complexes activate both C4 and C2. They cleave a peptide bond in C4 depositing C4b on the surface. They also cleave C2 into two fragments. The larger fragment (C2a) binds to C4b and forms the C3/C5 convertase enzyme complex C4b,C2a. This enzyme activates C3, deposits C3b on or near the C4b,C2a site and thus is converted from a weak C5 convertase to a highly efficient C5 convertase (C4b,C2a,C3b) with a Km for C5 3000-fold lower than that of the C4b,C2a enzyme alone (Rawal N. and Pangburn M.K. (2003)).
Source: Normal human serum (shown by certified tests to be negative for HBsAg and for antibodies to HCV, HIV-1 and HIV-II).
Species: Human
Form: Frozen liquid
Bio-activity: >90% versus normal human serum standard (see Cert of Analysis)
Molecular Mass: 93,000 Da (1 chain)
Purity: >95% by SDS-PAGE
Characteristic: Native human C2 is a naturally glycosylated polypeptide expressed as a 752 amino acid protein containing a 20 amino acid signal sequence. The mature protein contains 732 amino acids and is glycosylated at 8 potential sites all of which are N-linked sites (Morley, B.J. and Walport, M.J. (2000)). The calculated molecular weight of C2 is 81,000 daltons, but due to the high carbohydrate content (approximately 16%) it has been reported to run on reduced SDS-PAGE gels at a wide variety of apparent molecular weights. Depending on the SDS-PAGE system used C2 has been reported to appear as if it is 93,000, 102,000, 110,000, and 117,000 daltons. Upon cleavage of C2 by C1s or MASP two fragments are produced. The larger, C2a, with 509 amino acids forms the C3/C5 convertase of the classical and lectin pathways. C2a comes from the C-terminal of C2 while the smaller fragment, C2b, with 223 amino acids is from the N-terminal. Both contain carbohydrate. C2 has numerous allotypes (A, B, and C) and electrophoretic isoforms that can be separated by isoelectric focusing. The isoforms have pIs in the 6.0 to 6.3 pH range.
Usage: For research use only. Not for human or drug use.
Storage: -70°C or below. Avoid freeze/thaw.
Concentration: 0.5 mg/ml (see Certificate of Analysis for exact conc.)
Storage Buffer: 10 mM sodium phosphate, 145 mM NaCl, pH 6.0
Preservative: None, 0.22 μm filtered.
Warning: Use normal precautions for handling human blood products.
Gene Name: C2 complement component 2 [ Homo sapiens ]
Official Symbol: C2
Synonyms: C2; complement component 2; complement C2; C3/C5 convertase; complement component C2; CO2; DKFZp779M0311;
Gene ID: 717
mRNA Refseq: NM_000063
Protein Refseq: NP_000054
MIM: 613927
UniProt ID: P06681
Chromosome Location: 6p21.3
Pathway: Activation of C3 and C5, organism-specific biosystem; Complement Activation, Classical Pathway, organism-specific biosystem; Complement and Coagulation Cascades, organism-specific biosystem; Complement and coagulation cascades, organism-specific biosystem; Complement and coagulation cascades, conserved biosystem; Complement cascade, organism-specific biosystem; Immune System, organism-specific biosystem;
Function: peptidase activity; serine-type endopeptidase activity;

Online Inquiry

Note: There will be extra charge for optional service!
Optional requirements on this protein    +Expand
C-fusion    N-fusion   Non-tagged
His    GST   Fc   Others
<1.0 eu/μg    <0.1 eu/μg   <0.01 eu/μg   Not required
Monomer Isolation    Dimer Isolation    Not required
>80% by SDS-PAGE    >90% by SDS-PAGE   >95% by SDS-PAGE   Others

Please input "biomart" as verification code. Please review Creative BioMart's privacy policy for more information


Price does not include shipping and packaging costs.Request quote for final price.

Price Inquiry

Welcome! For price inquiries, please feel free to contact us through the form below. We will get back to you as soon as possible.