Human

E. coli

Expressed with an N-terminal Met.

Poly-His	IL-15 (Asn49-Ser162) Accession # P40933
N-term	C-term

IL15; IL-T; interleukin 15

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.

GenCrispr NLS-Cas9-EGFP is a fusion protein developed by GenScript. It contains a nuclear localization signal (NLS) on its N terminal end, and an EGFP and a 6x(His) sequence on the C terminal end. Cas9 nuclease is an RNA-guided endonuclease that can catalyze cleavage of double stranded DNA. This kind of targeted nuclease is a powerful tool for genome editing with high precision. Cas9 protein forms a highly stable ribonucleoprotein (RNP) complex with the guide RNA (gRNA) component of the CRISPR/Cas9 system. When Cas9 is expressed with an NLS sequence, the Cas9 RNP complex can localize to the nucleus immediately upon entering the cell. There is no requirement for in vivo transcription or translation, which improves the efficiency of this method over plasmid-based systems. Additionally, the Cas9 RNP complex is rapidly cleared from the cells minimizing the chance of off-target cleavage when compared to other systems (Kim, et al. 2014). The EGFP tag can be used as a reporter for tracking or sorting transfected cells, which enables enrichment of cell populations for desired genome edits via fluorescence activated cell sorting (FACS). It significantly reduces the labor and cost associated with single cell cloning and genotyping in genome editing applications.