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Immunology Innate Immunity Complement Classical Pathway

Recombinant Human C1QA protein (ab157982)

Recombinant Human C1QA protein (ab157982)
  • ChIP - Anti-Histone H3 antibody - Nuclear Loading Control and ChIP Grade (ab1791)

Key features and details

  • Expression system: Wheat germ
  • Tags: GST tag N-Terminus
  • Suitable for: ELISA, WB

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Description

  • Product name

    Recombinant Human C1QA protein
    See all C1QA proteins and peptides
  • Expression system

    Wheat germ
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      EDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGE PGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRR NPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEIC LSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPK KGHIYQGSEADSVFSGFLIFPSA
    • Amino acids

      23 to 245
    • Tags

      GST tag N-Terminus

Preparation and Storage

  • Alternative names

    • C1qa
    • C1QA_HUMAN
    • Complement C1q subcomponent subunit A
    • Complement component 1 q subcomponent A chain
    • Complement component 1 q subcomponent alpha polypeptide
    • Complement component C1q A chain
    see all
  • Function

    C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
  • Involvement in disease

    Defects in C1QA are the cause of complement component C1qA deficiency (C1QAD) [MIM:120550]. A rare defect resulting in C1 deficiency and impaired activation of the complement classical pathway. C1 deficiency generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis.
  • Sequence similarities

    Contains 1 C1q domain.
    Contains 1 collagen-like domain.
  • Post-translational
    modifications

    O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.
  • Cellular localization

    Secreted.
  • Target information above from: UniProt accession P02745 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

Images

  • SDS-PAGE - Recombinant Human C1QA protein (ab157982)
    SDS-PAGE - Recombinant Human C1QA protein (ab157982)
    ab157982 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact partnerships@abcam.com

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