biological source:
bacterial (Streptococcus sp.)
Quality Level: 100
Recombinant: expressed
in E. coli
Form: lyophilized
solid
mol wt: ~30 kDa
capacity: ~5 mg/mg,
solid binding capacity (IgG)
storage temp.: −20°C
General description
Genetically engineered truncated protein G; retains affinity
for IgG, but lacks albumin and Fab binding sites and membrane-binding regions.
Protein G, a cell wall protein,[1] is obtained from
group G streptococci.[2] The extracellular part of this protein is made of
two/three small domains or serum albumin binding (GA domains) and two/three
immunoglobulin (IgG) binding domains (B domains).[1]
Application
Protein G′ from Streptococcus sp. has been
used in in vitro actin labeling assay.[3]
Biochem/physiol Actions
Protein G can bind all the human and mouse IgG
subclasses.[2] It can bind to both the fragment crystallizable (Fc) and
antigen-binding fragment (Fab) components of the antibody.[1]
Physical form
lyophilized powder in a Tris-HCl buffer, pH 7.5