Active Recombinant Staphylococcal Protein A

• Cat.No.: COP32
• Product Overview: Recombinant Staphylococcal Protein A produced in E. Coli is a non-glycosylated, Polypeptide chain having a molecular mass of 45 kDa.

Specification

• Species: Staphylococcus
• Source: E.coli
• Tag: Non
• Description: Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).
• Molecular Mass: 45 kDa
• Physical Appearance: Sterile Filtered clear colorless solution.
• Formulation: The protein solution contains no additives.
• Purity: Greater than 98.0% as determined by RP-HPLC.
• Activity: Greater than 95.0% binding activity to human IgG.
• Stability: SPA should be stored at -20°C.
• Usage: Furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
• Introduction: Protein A is a 56 kDa MSCRAMM surface protein originally found in the cell wall of the bacterium Staphylococcus aureus. It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two-component system called ArlS-ArlR. It has found use in biochemical research because of its ability to bind immunoglobulins. It is composed of five homologous Ig-binding domains that fold into a three-helix bundle. Each domain is able to bind proteins from many of mammalian species, most notably IgGs. It binds the heavy chain with the Fc region of most immunoglobulins and also within the Fab region in the case of the human VH3 family. Through these interactions in serum, where IgG molecules are bound in the wrong orientation (in relation to normal antibody function), the bacteria disrupts opsonization and phagocytosis.
• Keywords: Immunoglobulin G-binding protein A; IgG-binding protein A; Staphylococcal protein A; SPA