Recombinant Human UBE2K (UBC1) Protein

Name: Recombinant Human UBE2K (UBC1) Protein
Brand: Beta LifeScience
SKU: BL-0125SG
Availability: InStock

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Product Overview

Tag	His
Host Species	Human
Accession	NM_005339
Synonym	E2-25K; HIP2; HYPG; LIG; UBC1
Background	UBE2K also known as UBC1 or ubiquitin-conjugating enzyme E2K belongs to the ubiquitin-conjugating enzyme family which interacts with RING finger proteins. UBE2K can ubiquitinate huntingtin, the gene product for Huntington's disease. Huntingtin is ubiquitinated in peripheral cells, suggesting a role for UBE2K in the degradation of huntingtin. UBE2K plays a role in aggregate formation of expanded polyglutamine proteins and the suppression of apoptosis in polyglutamine diseases. UBE2K also plays a role in the dislocation of newly synthesized MHC class I heavy chains from the endoplasmic reticulum, and involvement in foam cell formation.
Description	Recombinant full-length human UBE2K was produced in E. coli system, fused with a His tag at N-terminus.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	26 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
Bioactivity	Active
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 UBE2K (UBC1) 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	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	HGNC: 4914 OMIM: 602846 KEGG: hsa:3093 STRING: 9606.ENSP00000261427 UniGene: Hs.50308
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

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
Hip2, a ubiquitin-conjugating enzyme, can overcome radiation-induced G2/M cell cycle arrest and trigger the entry into mitosis. PMID: 23933584
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
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
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
This study suggests that Hip2 might be involved in the regulation of Smac-mediated apoptosis. PMID: 20537984
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
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.