Recombinant Streptococcal bacteria Protein G, His-tagged

• Cat.No.: Protein G-8140S
• Product Overview: Biotinylated Protein G (Biotinylated Protein G) was labeled with biotin based on Protein G Protein, which was produced in E.coli cells.

Specification

• Description: Protein G is an immunoglobulin-binding protein expressed in group C and G Streptococcal bacteria much like Protein A but with differing specificities. It is a 65-kDa (G148 protein G) and a 58 kDa (C40 protein G) cell surface protein that has found application in purifying antibodies through its binding to the Fc region. The native molecule also binds albumin, however, because serum albumin is a major contaminant of antibody sources, the albumin binding site has been removed from this recombinant form of Protein G. The primary amine of Protein G was labeled by biotin without decreasing its bioactivity, and has been used successfully for easy detection in ELISA, dot blot or Western blot, immunohistochemistry applications using streptavidin or avidin-conjugated probes. Biotin and other reactive related chemicals have been removed thoroughly by desalting after reaction termination.
• Source: E.coli
• Species: Streptococcal bacteria
• Tag: His
• Form: Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Trehalose are added as protectants before lyophilization.
• Molecular Mass: Biotinylated Protein G, fused with the polyhistidine tag at N-terminus and a single cysteine at C-terminus. DTT-reduced protein migrates as a 31 kDa polypeptide .The primary amine of Biotinylated Protein G was labeled by biotin for detection in ELISA, do
• Endotoxin: Less than 1.0 EU per μg of the Biotinylated Protein G by the LAL method.
• Purity: >95% as determined by reduced SDS-PAGE.
• Storage: Avoid repeated freeze-thaw cycles.No activity loss was observed after storage at:In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).
• Reconstitution: See Certificate of Analysis for details of reconstitution instruction and specific concentration.