Staphylococcal Protein A (SPA)

PEA1

SPN	Q129
PubMed	349081
UniProt	P23201
Wiki	Protein_A

Protein A is a 40-60 kDa MSCRAMM surface protein originally found in the cell wall of the bacteria 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 binds proteins from many of mammalian species, most notably IgGs. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. The result of this type of interaction is that, in serum, the bacteria will bind IgG molecules in the wrong orientation (in relation to normal antibody function) on their surface which disrupts opsonization and phagocytosis. It binds with high affinity to human IgG1 and IgG2 as well as mouse IgG2a and IgG2b. Protein A binds with moderate affinity to human IgM, IgA and IgE as well as to mouse IgG3 and IgG1.

Organism species: Pan-species (General)

PRODUCT TYPE	CATALOG NO.	PRODUCT NAME	APPLICATIONS
Proteins	N/A	Recombinant Staphylococcal Protein A (SPA)	Antigenic Transformation Customized Service Offer
Antibodies	N/A	Monoclonal Antibody to Staphylococcal Protein A (SPA)	Monoclonal Antibody Customized Service Offer
Antibodies	N/A	Polyclonal Antibody to Staphylococcal Protein A (SPA)	Polyclonal Antibody Customized Service Offer
Assay Kits	N/A	CLIA Kit for Staphylococcal Protein A (SPA)	CLIA Kit Customized Service Offer
Assay Kits	N/A	ELISA Kit for Staphylococcal Protein A (SPA)	ELISA Kit Customized Service Offer

Reference

"The SPA2 gene of Saccharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating."
J. Cell Biol. 111:1451-1464(1990) [PubMed] [Europe PMC] [Abstract]

"The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein."
Yeast 13:183-188(1997) [PubMed] [Europe PMC] [Abstract]

"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]

"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]

"Shs1p: a novel member of septin that interacts with spa2p, involved in polarized growth in Saccharomyces cerevisiae."
Biochem. Biophys. Res. Commun. 251:732-736(1998) [PubMed] [Europe PMC] [Abstract]

"Global analysis of protein expression in yeast."
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]

"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]

"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]

"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]

"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]