E. coli

Protein G; G Protein

Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Add 5 ml of distilled water to make the final concentration of 1 mg/ml

Protein G, a cell surface protein of group G streptococci, is a Type III Fc receptor that binds to the Fc region of IgG by a non-immune mechanism similar to that of protein A from Staphylococcus aureus. This product contains three IgG binding domains, but its albumin-binding region has been removed. Additionally, His-tag and cysteine have been added to N- and C-termini, respectively, to facilitate purification and conjugation. This does not affect the protein's ability to bind to IgG.

S. pyogenes

Recombinant Cas9 with an N-terminal NLS expressed by E.coli

10 mg/mL

GenCRISPR™ Ultra Cas9 is produced by expression in an E. coli strain carrying a plasmid encoding the Cas9 gene from Streptococcus pyogenes with an N-terminal nuclear localization signal (NLS).

S. pyogenes

Recombinant Cas9 with double-ended NLS expressed by E.coli

10 mg/mL

GenCRISPR™ Ultra eSpCas9-2NLS is a mutant form of Cas9 nuclease and is produced by expression in an E. coli strain carrying a plasmid encoding the eSpCas9 gene from Streptococcus pyogenes with double-ended nuclear localization signal (NLS). GenCRISPR™ Ultra eSpCas9-2NLS delivers higher fidelity and less off-target activity than wild-type SpCas9 nuclease.

rTEV, TEV, P1 protease

Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the Tobacco Etch Virus (TEV). The optimum recognition site for this enzyme is the sequence Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) [ENLYFQ(G/S)] and cleavage occurs between the Gln and Gly/Ser residues, The most commonly used sequence is ENLYFQG. The protease is used to cleave affinity Tobacco Etch Virus Protease (rTEV) contains 231 amino acids with N-terminal His tagged. A fully biologically active molecule, rTEV has a molecular mass of 28.4 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Human Rhinovirus

rPSP, PSP, HRV 3C Protease

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin.Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

IgG1 for MAbs D31

CA72-4 (Cancer antigen 72-4), also known as Tumor associated glycoprotein (TAG) 72, is a mucin-like protein of high molecular weight (200- 400 kD). CA 72-4 has high specificity for diagnosis of benign diseases. It is also a helpful marker in the diagnosis of gastric cancer, ovarian carcinoma and colorectal carcinoma.