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CC-154

ARG2 Easy KO Kit

For research use only. Not intended for any clinical use.

Cat. No. :   CC-154

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Product Information

Gene Information

Cat. No. CC-154
Description A complete kit for efficient gene knockout in mammalian cells, combining chemically synthesized sgRNAs with Cas9 RNPs to induce targeted DNA cleavage and generate frameshift mutations or deletions. All essential reagents for transfection and knockout validation are included for rapid, high-efficiency gene disruption.
Gene Abbr ARG2
Species Human
Ensembl ID ENSG00000081181
NCBIGene ID 384
Uni Prot ID P78540
Features
  • All-in-One workflow from gene editing to knockout validation for users with no prior experience.
  • Pre-validated sgRNAs and primers for rapid setup.
  • Streamlined experiment handling.
  • CRISPR RNP method ensures precise and efficient gene knockout.
Applications This kit enables in vitro gene knockout in human-derived cells using chemically synthesized sgRNAs and Cas9-gRNA RNP complexes. Transfected RNPs cleave early exons of the target gene, inducing deletions or frameshift mutations for efficient and rapid knockout.
Reactions 5–10 reactions per target gene
Kit Components 2–3 chemically synthesized sgRNAs (200pmol each)
3 PCR/Sequencing primers (500pmol each)
LM cell lysate (500µL)
Cas9 protein (12µg)
LM RNP transfection reagent (50µL)
Storage Store at -80°C for up to 1 year or at -20°C for up to 6 months. Avoid repeated freeze-thaw cycles.
Target Gene ARG2
Background Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exists (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type II isoform encoded by this gene, is located in the mitochondria and expressed in extra-hepatic tissues, especially kidney. The physiologic role of this isoform is poorly understood; it is thought to play a role in nitric oxide and polyamine metabolism. Transcript variants of the type II gene resulting from the use of alternative polyadenylation sites have been described. [provided by RefSeq, Jul 2008]
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