Nacetyltransferase 6 protein (His tag) (80R-1126)
Purified recombinant Human Nacetyltransferase 6 protein
|Synonyms||FUS2 protein, FUS 2 protein, Nacetyltransferase -6 protein, FUS-2 protein, Nacetyltransferase -6, Protein fusion-2 protein, N acetyltransferase 6 protein, Nacetyltransferase 6, Protein fus 2 protein, Nacetyltransferase 6 protein, NAT6 protein, Nacetyltransferase 6, Protein fusion 2.|
Coomassie Blue stained SDS-PAGE of Nacetyltransferase 6 protein (His tag) (80R-1126)
Figure annotation denotes ug of protein loaded and % gel used.
|Residues||1-308 amino acids: MGSSHHHHHH SSGLVPRGSH MQELTLSPGP AKLTPTLDPT HRMELILSTS PAELTLDPAC QPKLPLDSTC QPEMTFNPGP TELTLDPEHQ PEETPAPSLA ELTLEPVHRR PELLDACADL INDQWPRSRT SRLHSLGQSS DAFPLCLMLL SPHPTLEAAP VVVGHARLSR VLNQPQSLLV ETVVVARALR GRGFGRRLME GLEVFARARG FRKLHLTTHD QVHFYTHLGY QLGEPVQGLV FTSRRLPATL LNAFPTAPSP RPPRKAPNLT AQAAPRGPKG PPLPPPPPLP ECLTISPPVP SGPPSKSLLE TQYQNVRGRP IFWMEKDI|
|Grade & Purity||> 95% pure|
|Molecular Weight||35.9 kDa (328aa), confirmed by MALDI-TOF. (Molecular weight on SDS-PAGE will appear higher)|
|Form & Buffer||Supplied as a liquid in 20mM Tris-HCl buffer, pH 8.0, containing 100mM NaCl, and 20% glycerol.|
Storage & Safety
|Storage||Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|Biological Significance||N-acetyltransferase, also known as FUS2 (NAT6), is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. This enzyme is physically localized in the cytoplasm and its activity has been documented by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Since the Fus-2 gene maps to the chromosomal region 3p21.3, which contains at least one tumor suppressor gene, the N-acetyltransferase functions of Fus-2 may be relevant to its potential role in cancer. Recombinant human N-acetyltransferase 6 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography.|
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