Recombinant Human UBA2 (SAE2) Protein

Beta LifeScience SKU/CAT #: BL-1253SG

Recombinant Human UBA2 (SAE2) Protein

Beta LifeScience SKU/CAT #: BL-1253SG
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Product Overview

Tag GST
Host Species Human
Accession NM_005499
Synonym UBA2; UBLE1B; SAE2; ARX; HRIHFB2115
Background UBA2 (SAE2) or ubiquitin-like modifier activating enzyme 2 forms a heterodimer that functions as a SUMO-activating enzyme for the sumoylation of proteins. The posttranslational modification of proteins by the addition of the small protein SUMO or sumoylation, regulates protein structure and intracellular localization (1). UBA2 functions in SUMO1 activation in a manner analogous to the single E1 ubiquitin-activating enzymes (2). The inactivation of UBA2 may be a therapeutic strategy in MYC-driven cancers.
Description Recombinant full-length human UBA2 (SAE2) was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source Sf9 insect cells
AA Sequence Full Length
Molecular Weight ~115 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human UBA2 (SAE2) Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.
Subcellular Location Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.
Protein Families Ubiquitin-activating E1 family
Database References

HGNC: 30661

OMIM: 613295

KEGG: hsa:10054

STRING: 9606.ENSP00000246548

UniGene: PMID: 29231810

  • We propose that disturbance of the SUMOylation pathway, mediated by pathogenic variants in UBA2, is a novel mechanism for aplasia cutis congenita and other phenotypic abnormalities. PMID: 28110515
  • Here, we show that hHR23A utilizes both the UBA2 and XPCB domains to form a stable complex with Vpr, linking Vpr directly to cellular DNA repair pathways and their probable exploitation by the virus. PMID: 24318982
  • This study has identified the mechanism used to localize SAE to the nucleus. PMID: 23095757
  • Data indicate the role of anti-SUMO activating enzyme SAE1 and SAE2 antibody as marker of dermatomyositis. PMID: 22884621
  • Data show that the SAE2 subunit of the small ubiquitin-like modifier (SUMO) E1 is autoSUMOylated at residue Lys-236, and SUMOylation was catalyzed by Ubc9 at several additional Lys residues surrounding the catalytic Cys-173 of SAE2. PMID: 22403398
  • loss of SAE1/2 activity drives synthetic lethality with Myc; inactivation of SAE2 leads to mitotic catastrophe and cell death upon Myc hyperactivation; findings in Myc-high breast cancers suggest low tumor SAE1 and SAE2 correlates metastasis-free survival PMID: 22157079
  • The mammalian E1 subunits can be imported separately, identify nuclear localization signals (NLSs) in Aos1 and in Uba2, and demonstrate that their import is mediated by importin alpha/beta in vitro and in intact cells. PMID: 21209321
  • structures of heterodimeric Sae1/Sae2-Mg.ATP and Sae1/Sae2-SUMO-1-Mg.ATP complexes PMID: 15660128
  • UBA2 stabilizes APOBEC3G by preventing ubiquitin chain elongation and proteasome-mediated proteolysis. PMID: 18680593
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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