Recombinant Human UBC9 Protein

Beta LifeScience SKU/CAT #: BLPSN-4710

Recombinant Human UBC9 Protein

Beta LifeScience SKU/CAT #: BLPSN-4710
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Product Overview

Tag N/A
Host Species Human
Accession P63279
Synonym C358B7.1, P18, UBC9
Background UBE2I is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by an ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.
Description A DNA sequence encoding the human UBE2I (P63279) (Met 1-Ser 158) was expressed and purified, with additional two amino acids (Gly & Pro) at the N-terminus.
Source E.coli
Predicted N Terminal Gly
AA Sequence Met 1-Ser 158
Molecular Weight The recombinant human UBE2I consists of 160 a.a. and migrates as an approximately 18 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, 10% glycerol, 2mM DTT, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity.
Subcellular Location Nucleus. Cytoplasm.
Protein Families Ubiquitin-conjugating enzyme family
Database References
Tissue Specificity Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus.

Gene Functions References

  1. Study demonstrated overexpression of Ubc9 protein in osteosarcoma. Silencing Ubc9 in osteosarcoma cell lines induced decoupling of SUMO1 from Cx43, generating increased free Cx43 levels, which is important for reconstructing gap junction intercellular communication and recovering cellular functions. PMID: 29956745
  2. Data show that the forkhead Box Protein P3 (FOXP3) response element at the -310 bp region, but not the -2182 bp region, is mainly required for ubiquitin conjugating enzyme 9 (UBC9) activation by FOXP3. PMID: 30011797
  3. Study provides an insight into the role of the RNF4 to balance the role of SUMO signaling by directly targeting Ubc9 and SUMO E3 ligases. PMID: 29180619
  4. The SUMO1/UBC9 axis may regulate Nox1mediated diabetic retinopathy by inhibiting reactive oxygen species generation and apoptosis. PMID: 29138839
  5. our results indicate that down-regulation of UBC9 sensitizes cells to anticancer drugs, is possibly associated with the regulation of ERK1/2 and P38 activation and interacts with the intrinsic apoptosis pathway. PMID: 28572537
  6. Ubc9 is an essential regulator of ADAP where it is required for TCR-induced membrane recruitment of the small GTPase Rap1 and its effector protein RapL and for activation of the small GTPase Rac1 in T cell adhesion. PMID: 29127148
  7. NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division. PMID: 28900032
  8. Listeriolysin O -induced down-regulation of Ubc9 is independent of Ubc9-SUMO interaction, however, it may involve phosphorylation signaling. PMID: 28911869
  9. Sumoylation of PML with SUMO2 by UBC9/UBE2I can lead to formation of polymeric SUMO chains. Data suggest that coordination of growing poly-SUMO chain with "back side" binding site on UBC9/UBE2I appears to be required for SUMO chain elongation on PML. (PML = promyelocytic leukemia protein; SUMO2 = small ubiquitin-like modifier 2; UBC9/UBE2I = ubiquitin-conjugating enzyme UBC9/UBE2I) PMID: 28784659
  10. The role of Transthyretin in the regulation of Ubc9 SUMOylation PMID: 27501389
  11. These findings point to UBC9 and autophagy as novel hallmarks of human papillomavirus oncogenesis PMID: 28253371
  12. These findings reveal that SUMO E1~E2 oxidation is an essential redox switch in oxidative stress. PMID: 27174643
  13. the mRNA and protein expression of Ubc9 are regulated by the microRNA miRNA-30a (miR-30a) in human subcutaneous adipocytes. PMID: 27758866
  14. miR-30e in VSMCs exerted an anti-atherosclerosis effect via inhibiting proliferation and migration, and promoting apoptosis of VSMCs. More specifically, it was demonstrated that miR-30e exhibited these effects on VSMCs partially through targeting Ube2i and downregulating the IkappaBalpha/NFkappaB signaling pathway. PMID: 28123167
  15. Ubc9 plays different roles of action in antitumor agents in chemotherapy. The process requires bleomycin hydrolase and poly(ADP-ribose) polymerase-1. The results are beneficial to deeply understanding of Ubc9 functions and for precise prediction of chemotherapy outcomes in tumors. PMID: 27878232
  16. Suggest a novel role of PCGF2 in arsenic trioxide-mediated degradation of PML-RARA that PCGF2 might act as a negative regulator of UBE2I via direct interaction. PMID: 27030546
  17. Akt directly phosphorylates Ubc9 at Thr35 and phosphorylates SUMO1 at Thr76. Ubc9 phosphorylation at Thr35 promotes Ubc9 thioester bond formation and SUMO1 phosphorylation at Thr76 stabilizes the SUMO1 protein. PMID: 25867063
  18. Characterization and Structural Insights into Selective E1-E2 Interactions in the Human and Plasmodium falciparum SUMO Conjugation Systems. PMID: 26697886
  19. a high-throughput microscopy screen identified ubiquitin carrier protein 9 (Ubc9) as a negative regulator of energy storage in human sc adipocytes. Ubc9 depletion enhanced energy storage and induced the brown fat gene program in human sc adipocytes. PMID: 26192107
  20. The authors show that ZNF451 is SUMO2 specific and that SUMO modification of ZNF451 may contribute to activity by providing a second molecule of SUMO that interacts with E2. PMID: 26524494
  21. The RWD domain binds to a Ubc9 surface that also must interact with E1, E3, and SUMO. PMID: 25918163
  22. These data show that NS5A is a target protein of small ubiquitin-like modifier (SUMO) and is SUMOylated at lysine residue 348 and silencing of UBC9 impaired hepatitis C virus replication. PMID: 24602294
  23. SUMO E2 ligase Ubc9 has a critical role in oncogenesis driven by the Ras/Raf pathway PMID: 25805818
  24. Ubc9 gene plays an important role in cell proliferation in epithelial ovarian cancer through PI3K/Akt signaling pathway. PMID: 23708104
  25. Data indicate that protein tyrosine phosphatase 1B (PTP1B) association with calnexin is ubiquitin conjugating enzyme 9 (UBC9)-dependent. PMID: 25586181
  26. N-terminal amino acid residues of Ubc9 are critical for Ubc9 nuclear enrichment and localization. PMID: 25637535
  27. the Ran system and Ubc9 are functionally coupled to the structure of the nuclear lamina and reactive oxygen species production through feedback loops PMID: 24523287
  28. Although E2 approximately SUMO-1 exhibits no specificity for product-bound TDG, the relatively high conjugation efficiency raises the possibility that E2-mediated sumoylation could stimulate product release in vivo. PMID: 24753249
  29. The variability of the UBC9 gene can play a role in breast cancer occurrence. PMID: 23873416
  30. UBC9 appears to play an important role in the tumor biology of Nigerian women. PMID: 24176171
  31. miR-214 and its target gene UBC9 may contribute to the development and the clinical outcome of glioma PMID: 24277415
  32. The proximal UBC9 promoter. PMID: 24086615
  33. Study showed that ZHX1 is SUMOylated by Ubc9 with SUMO1 at the sites K159, K454, and K626 and that the SUMOylation of ZHX1 regulated the stability, ubiquitination and transcriptional activity of ZHX1. PMID: 23686912
  34. This study provides further insight in the processing and packaging of the HIV-1 gp120 into mature HIV-1 virions. PMID: 23861967
  35. We observed steady-state expression of SUMO-conjugated enzyme-UBC9 throughout normal gestation. Placental UBC9 levels were strikingly increased in severe pre-eclampsia patients. PMID: 23628505
  36. These results suggest that the SUMOylation of DDB2 facilitates CPD repair. PMID: 23860269
  37. we demonstrated that upregulation of Ubc9 expression promotes migration and invasion. Ubc9 likely plays an important role in cancer progression by promoting invasion and metastasis in lung cancer. PMID: 23381475
  38. High UBC9 expression is associated with glioma. PMID: 23187003
  39. From these observations, we concluded that UBC9 is a novel regulator of the mammalian ER stress response. PMID: 23470653
  40. The E2 enzyme Ubc9 is an interaction partner of E1B-55K, providing a possible molecular explanation for SUMO-dependent modulation of cellular target proteins. PMID: 22614022
  41. A previously undescribed SIRT1/Ubc9 regulatory axis in the modulation of protein sumoylation and the hypoxia response. PMID: 23395904
  42. High Ubc9 expression correlates with poor response to chemotherapy and poor clinical prognosis in breast cancer. PMID: 21880185
  43. 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
  44. UBC9 protein expression is reduced in muscle from type 2 diabetic patients with severe insulin resistance. PMID: 22114711
  45. There was no statistical association of UBE2I expression between human epithelial ovarian cancer tumor and normal tissues PMID: 21971700
  46. Ubc9 and PIAS1 potentiated SF-1-mediated transactivation of human CYP17, CYP11A1, and CYP11B1 but not CYP11B2 promoters. PMID: 21467194
  47. Binding of BRCA1 proteins to nuclear chaperone Ubc9 provides a novel mechanism for nuclear import and control of tumor growth. PMID: 21344391
  48. The authors propose that LMP1, by interaction with Ubc9, modulates sumoylation processes, which regulate signal transduction pathways that affect phenotypic changes associated with oncogenesis. PMID: 21795333
  49. The authors report that the high risk human papillomavirus E6 proteins reduce the intracellular quantity of the sole SUMO conjugation enzyme, Ubc9, concomitant with decreased host sumoylation. PMID: 21510985
  50. Analysis of the dynamics of E2(Ubc9)-SUMO-Target(RanGAP1) in the absence and presence of E3(RanBP2) revealed that two different allosteric sites regulate the ligase activity. PMID: 21216249


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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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