| Product Name | UBA3, 1-463aa, Human |
|---|---|
| Description | UBA3, also known as NEDD8-activating enzyme E1 catalytic subunit, is the catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Recombinant human UBA3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. |
| Synonyms | NEDD8-activating enzyme E1 catalytic subunit, UBE1C |
| Host | E. coli |
| Molecular Weight | 39.8 kDa(348aa) confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSHMADGEE PERKRRRIEE LLAEKMAVDG GCGDTGDWEG RWNHVKKFLE RSGPFTHPDF EPSTESLQFL LDTCKVLVIG AGGLGCELLK NLALSGFRQI HVIDMDTIDV SNLNRQFLFR PKDIGRPKAE VAAEFLNDRV PNCNVVPHFN KIQDFNDTFY RQFHIIVCGL DSIIARRWIN GMLISLLNYE DGVLDPSSIV PLIDGGTEGF KGNARVILPG MTACIECTLE LYPPQVNFPM CTIASMPRLP EHCIEYVRML QWPKEQPFGE GVPLDGDDPE HIQWIFQKSL ERASQYNIRG VTYRLTQGVV KRIIPAVAST NAVIAAVCAT EVFKIATSAY IPLNNYLVFN DVDGLYTYTF EAERKENCPA CSQLPQNIQF SPSAKLQEVL DYLTNSASLQ MKSPAITATL EGKNRTLYLQ SVTSIEERTR PNLSKTLKEL GLVDGQELAV ADVTTPQTVL FKLHFTS |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol 1mM DTT, 0.1M NaCl |
| Concentration | 1.0 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Gong L., et al. (1999) J. Biol. Chem. 274:12036-12042 Bohnsack R.N., et al. (2003) J. Biol. Chem. 278:26823-26830 |
| Background | UBA3, also known as NEDD8-activating enzyme E1 catalytic subunit, is the catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Recombinant human UBA3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. |
| Supplier | ARP |
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