FUS2/NAA80 (AA 1-308) protein (His tag)
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- Target
- FUS2/NAA80
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-308
- Origin
- Human
- Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- His tag
- Application
- SDS-PAGE (SDS)
- Sequence
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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 - Characteristics
- N-acetyltransferase 6, 1-308 aa, Human, His-tagged, Recombinant, E.coli
- Purity
- > 95% by SDS-PAGE
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.5 mg/mL
- Buffer
- Liquid. In 20 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl 20% glycerol.
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Avoid repeated freezing and thawing cycles.
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- Target
- FUS2/NAA80
- Background
- 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.
- Molecular Weight
- 35.9 kDa (328aa) confirmed by MALDI-TOF (Molecular weight on SDS-PAGE will appear higher)
- NCBI Accession
- NP_036323
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