Human SAE1 Protein (His & GST Tag)

AOS1,HSPC140,SUA1,UBLE1A

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Catalog Number	P13921-H20B
Organism Species	Human
Host	Baculovirus-Insect Cells
Synonyms	AOS1,HSPC140,SUA1,UBLE1A
Molecular Weight	The recombinant human SAE1 /GST chimera consists of 583 amino acids and has a calculated molecular mass of 66.3 kDa. The recombinant protein migrates as an approximately 61 kDa band in SDS-PAGE under reducing conditions.
predicted N	Met
SDS-PAGE
Purity	> 95 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human SAE1 (Q9UBE0) (Met1-Lys346) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Bio-activity
Research Area	Immunology |Signal Transduction |ITIM/ITAM Immunoreceptors and Related Molecules
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% gly 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	SAE1 belongs to the ubiquitin-activating E1 family. It is a heterodimer that acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It functions as a UBLI E1 ligase mediating the ATP-dependent activation of UBL1. SAE1 binds with UBLE1A and UBLE1B to form a heterodimer which can bind UBL1. SAE1 also regulates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2. SAE1 and UBA2 form a heterodimer that functions as a SUMO-activating enzyme for the sumoylation of proteins.
Reference	Gong L, et al. (1999) Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex. FEBS Lett. 448(1):185-9. Lois LM, et al. (2005) Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. EMBO J. 24(3):439-51. Tatham MH, et al. (2001) Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J Biol Chem. 276(38):35368-74.