Recombinant Human Sumo-Activating Enzyme Subunit 2 (UBA2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-11205P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Sumo-Activating Enzyme Subunit 2 (UBA2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-11205P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Sumo-Activating Enzyme Subunit 2 (UBA2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q9UBT2
Target Symbol UBA2
Synonyms Anthracycline associated resistance ARX; Anthracycline-associated resistance ARX; ARX; FLJ13058; HRIHFB2115; SAE 2; SAE2; SAE2_HUMAN; SUMO 1 activating enzyme subunit 2; SUMO activating enzyme subunit 2; SUMO-activating enzyme subunit 2; UBA2; UBA2 ubiquitin activating enzyme E1 homolog; Ubiquitin like 1 activating enzyme E1B; Ubiquitin like modifier activating enzyme 2; Ubiquitin-like 1-activating enzyme E1B; UBLE1B
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEARARASNEDGDIKRISTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEETNASDQQNEPQLGLKDQQVLDVKSYARLFSKSIETLRVHLAEKGDGAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQPNPRKKLLVPCALDPPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEANNHKKLSEFGIRNGSRLQADDFLQDYTLLINILHSEDLGKDVEFEVVGDAPEKVGPKQAEDAAKSITNGSDDGAQPSTSTAQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLDEKENLSAKRSRIEQKEELDDVIALD
Expression Range 1-640aa
Protein Length Full Length
Mol. Weight 84.2 kDa
Research Area Cell Biology
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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

Gene Functions References

  1. Calcium/calpain-induced cleavage of the SAE2 leads to sumoylation inhibition reslting in bacillary dysentery. PMID: 29231810
  2. 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
  3. 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
  4. This study has identified the mechanism used to localize SAE to the nucleus. PMID: 23095757
  5. Data indicate the role of anti-SUMO activating enzyme SAE1 and SAE2 antibody as marker of dermatomyositis. PMID: 22884621
  6. 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
  7. 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
  8. 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
  9. structures of heterodimeric Sae1/Sae2-Mg.ATP and Sae1/Sae2-SUMO-1-Mg.ATP complexes PMID: 15660128
  10. 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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