Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Isolation of cDNA clones for human complement component C2.

D R Bentley, R R Porter

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Interactions of complement components with antibody - antigen aggregates and cell surfaces.

    Immunology today·2014
    Same author

    Complement system proteins which interact with C3b or C4b A superfamily of structurally related proteins.

    Immunology today·2014
    Same author

    Some electrolyte considerations in the field of surgery.

    The Southern surgeon·2014
    Same author

    Muscle Biopsy in the Study of Electrolyte Changes, with Particular Reference to Chronic Renal Disease.

    Transactions of the American Clinical and Climatological Association·2011
    Same author

    HEART-BLOCK IN A CASE OF PNEUMONIA.

    British medical journal·2010
    Same author

    The DNA sequence and biological annotation of human chromosome 1.

    Nature·2006
    Same journal

    The TaMYB55-TaSnRK1α1-TabZIP9 module confers heat stress tolerance in wheat.

    Proceedings of the National Academy of Sciences of the United States of America·2026
    Same journal

    Superstatistics approach to turbulent circulation fluctuations.

    Proceedings of the National Academy of Sciences of the United States of America·2026
    Same journal

    A molecular timescale for evolution of cobamide biosynthesis.

    Proceedings of the National Academy of Sciences of the United States of America·2026
    Same journal

    Pierre Chambon, a pioneer of molecular biology and gene regulation in eukaryotes.

    Proceedings of the National Academy of Sciences of the United States of America·2026
    Same journal

    Granulosa cell glycogen fuels the avascular corpus luteum.

    Proceedings of the National Academy of Sciences of the United States of America·2026
    Same journal

    Synthetic essentiality of TRAIL/TNFSF10 in VHL-deficient renal cell carcinoma.

    Proceedings of the National Academy of Sciences of the United States of America·2026
    See all related articles

    Researchers isolated human complement component C2 (C2) cDNA clones, revealing a 400-base-pair insert coding for the serine protease active site. This region showed homology to factor B, with a C2 mRNA size of 2.9 kilobases identified.

    Area of Science:

    • Molecular Biology
    • Immunology
    • Genetics

    Background:

    • Complement component C2 (C2) is a crucial protein in the complement system, involved in immune responses.
    • Understanding the genetic and molecular basis of C2 is essential for comprehending immune system function and related disorders.

    Purpose of the Study:

    • To isolate and characterize cDNA clones encoding human complement component C2.
    • To investigate the structural and functional relationship between C2 and related serine proteases like factor B.
    • To determine the size of C2 mRNA and analyze the C2 gene locus.

    Main Methods:

    • Screening a human liver cDNA library using a mixture of synthetic oligonucleotides.
    • RNA transfer (Northern blot) analysis to determine mRNA size.

    Related Experiment Videos

  • Southern blot analysis of genomic DNA to identify the C2 gene locus.

    • Main Results:

    • Two human complement component C2 (C2) cDNA clones were isolated.
    • A 400-base-pair insert (pC201) codes for the serine protease active site and substrate binding pocket.
    • This region exhibits 34% homology to human factor B, with conserved amino acid replacements.
    • C2 mRNA is approximately 2.9 kilobases in size.
    • Southern blot analysis confirmed a single C2 locus without cross-hybridization to the factor B locus.

    Conclusions:

    • The isolated cDNA clones provide valuable tools for studying complement component C2.
    • The identified homology suggests a shared evolutionary origin and functional relationship between C2 and factor B.
    • The characterization of C2 mRNA size and gene locus provides fundamental data for further genetic and immunological research.