Labeling-detection

Protein A, recombinant

  • Cat.Number : AS-72233-5
  • Availability :
    In stock
  • Shipping conditions : Ice fees will apply

Size

Quantity

Protein A is a non-glycosylated cell wall protein of Staphylococcus aureus that can bind Fc part of immunoglobulin molecule of different species with strong affinity. Protein A consists of five IgG binding domains (A, B, C, D, and E) each is approximately 60 amino acids long with no cysteines present and two Staphylococcus aureus cell membrane binding domains (X and M).
AnaSpec's recombinant Protein A consists of only IgG binding domains and was expressed in E. coli. Its apparent molecular mass is approximately 30,000 Da compared to 42,000 Da for the native Protein A that is found in Staphylococcus aureus. Recombinant Protein A can be used for immunoprecipitation, antibodies purification, and assay development.
It is provided as a 25 mg/mL sterile salt-free liquid form.

Specifications

Chemistry
Molecular Mass/ Weight
  • ~30000
Quantity & Purity
Concentration
  • 25 mg/mL
Purity
  • ≥95% by SDS-PAGE
Storage & stability
Form
  • In solution
Storage Buffer
  • Sterile salt-free liquid
Storage Conditions
  • Protein A is stable for 1-2 weeks at 4°C. For long-term storage, divide the solution into aliquots and store at -20°C or add an equal volume of glycerol and store at -20°C without aliquoting. Avoid multiple thaw-freeze cycles.
Activity
Application
Biomarker Target
Usage
  • Research use
Source
Host
Source / Species
  • E. coli

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References

Interaction between streptococcal IgG Fc receptors and human and rabbit IgG domains.

Immunol . 1986 Feb 01 ; 57 305 | DOI : 1453956

  • A.K. Schröder
  • et al

Structural Studies on the Four Repetitive Fc-Binding Regions in Protein A from Staphylococcus aureus

Eur J Biochem . 1977 Sep 01 ; 78(2) 471 | DOI : https://doi.org/10.1111/j.1432-1033.1977.tb11760.x

  • J. Sjödahl

Some Physicochemical Properties of Protein A from Staphylococcus aureus

Eur J Biochem . 1972 Sep 01 ; 29(3) 579 | DOI : https://doi.org/10.1111/j.1432-1033.1972.tb02024.x

  • I. Björk
  • et al