Recombinant Human UBE2K Protein (N-6His, SUMO tag)

Beta LifeScience SKU/CAT #: BL-2062NP
BL-2062NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
BL-2062NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human UBE2K Protein (N-6His, SUMO tag)

Beta LifeScience SKU/CAT #: BL-2062NP
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Product Overview

Description Recombinant Human Ubiquitin-Conjugating Enzyme E2 K is produced by our E.coli expression system and the target gene encoding Met1-Asn200 is expressed with a 6His, SUMO tag at the N-terminus.
Accession P61086
Synonym Ubiquitin-Conjugating Enzyme E2 K; Huntingtin-Interacting Protein 2; HIP-2; Ubiquitin Carrier Protein; Ubiquitin-Conjugating Enzyme E2-25 kDa; Ubiquitin-Conjugating Enzyme E2(25K); Ubiquitin-Conjugating Enzyme E2-25K; Ubiquitin-Protein Ligase; UBE2K; HIP2; LIG
Gene Background Ubiquitin-Conjugating Enzyme E2 K (UBE2K) belongs to the E2 Ubiquitin-Conjugating Enzyme family. UBE2K is highly expressed in the brain, with highest levels found in cortex and striatum, and at lower levels in cerebellum and brainstem. UBE2K may mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. UBE2K is associated with the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with huntingtin, and MHC-heavy chain proteins.
Molecular Mass 34.5 KDa
Apmol Mass 38 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.
Subcellular Location Cytoplasm.
Protein Families Ubiquitin-conjugating enzyme family
Database References
Tissue Specificity Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest leve

Gene Functions References

  1. The crystal structure of a Ube2K~ubiquitin conjugate has been described, and it was shown that even though it is monomeric, Ube2K can synthesize Lys48-linked ubiquitin chains. PMID: 26592444
  2. Hip2, a ubiquitin-conjugating enzyme, can overcome radiation-induced G2/M cell cycle arrest and trigger the entry into mitosis. PMID: 23933584
  3. An extract of bark from the tropical rainforest plant Byrsonima crassifolia was screened for inhibition of diubiquitin formation by the human ubiquitin-conjugating enzyme E2-25K. PMID: 22164771
  4. one of the roles of the C-terminal UBA domain, in the context of E2-25K, is to increase processivity in Lys48-linked polyubiquitin chain synthesis, possibly through increased binding to the ubiquitinated substrate. PMID: 21281599
  5. Results suggest that the interaction between E2-25K and UBB(+1) is critical for the synthesis and accumulation of UBB(+1)-anchored polyubiquitin, which results in proteasomal inhibition and neuronal cell death. PMID: 20826778
  6. This study suggests that Hip2 might be involved in the regulation of Smac-mediated apoptosis. PMID: 20537984
  7. Results suggest that in permeabilized, US11-expressing cells polyubiquitination of the MHC class I heavy chain substrate can be catalyzed by E2-25K. PMID: 16868077
  8. E2-25K is involved in aggregate formation of expanded polyglutamine proteins and polyglutamine-induced cell death. PMID: 17092742

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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