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AB269098

Recombinant human UBE2D3 protein (Active)

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Recombinant human UBE2D3 protein (Active) is a Human Full Length protein, in the 1 to 147 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.

View Alternative Names

UBC5C, UBCH5C, UBE2D3, Ubiquitin-conjugating enzyme E2 D3, (E3-independent) E2 ubiquitin-conjugating enzyme D3, E2 ubiquitin-conjugating enzyme D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2(17)KB 3, Ubiquitin-conjugating enzyme E2-17 kDa 3, Ubiquitin-protein ligase D3

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Functional Studies - Recombinant human UBE2D3 protein (Active) (AB269098)
  • FuncS

Supplier Data

Functional Studies - Recombinant human UBE2D3 protein (Active) (AB269098)

The specific activity of ab269098 was determined to be 17 nmol/min/mg in a ubiquitinating assay using wild-type ubiqutin protein as substrate.

SDS-PAGE - Recombinant human UBE2D3 protein (Active) (AB269098)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human UBE2D3 protein (Active) (AB269098)

SDS-PAGE analysis of ab269098.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

The specific activity of ab269098 was determined to be 17 nmol/min/mg in a ubiquitinating assay using wild-type ubiqutin protein as substrate.

Accession

P61077

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7 Preservative: 1.02% Imidazole Constituents: 25% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":147,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P61077","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

UBE2D3 also known as UbcH5c or E2-17k is a ubiquitin-conjugating enzyme. It plays a critical role in the ubiquitination process by interacting with ligase enzymes adding ubiquitin to target proteins. This protein has a molecular mass of approximately 16 kDa. UBE2D3 is widely expressed in various tissues indicating its role in several cellular functions.
Biological function summary

UBE2D3 acts as an important component in protein degradation and regulation. It participates in the ubiquitin-proteasome system which controls protein levels in cells. UBE2D3 forms part of larger protein complexes such as the SCF (Skp Cullin F-box containing) complex contributing to the regulation of cell cycle and signal transduction. This interaction helps control cell division and response to external signals.

Pathways

UBE2D3 plays an important role in the NF-kB signaling and DNA damage response pathways. It interacts with proteins such as IKK (IκB kinase) to regulate inflammation and immune response. Additionally UBE2D3's involvement in the DNA repair pathway supports maintaining genome stability by collaborating with other proteins like BRCA1 which is essential for repairing DNA double-strand breaks.

UBE2D3 shows a connection to cancer and neurodegenerative diseases. Its role in the NF-kB signaling pathway links it to cancer development due to its regulation of genes involved in cell growth and survival. In neurodegenerative disorders such as Alzheimer's disease abnormal ubiquitination due to UBE2D3 dysfunction may lead to protein aggregation affecting normal cellular activities. Its interaction with proteins like p53 a well-known tumor suppressor illustrates its importance in disease progression and regulation.
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Specifications

Form

Liquid

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General info

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592, PubMed : 28322253). In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592). Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed : 20347421). Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin (PubMed : 10329681). Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin (PubMed : 10329681). Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA (PubMed : 18948756). Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase (PubMed : 18948756). Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair (PubMed : 16628214). Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus (PubMed : 18515077). In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53 (PubMed : 12646252, PubMed : 15280377). In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes (PubMed : 18508924). In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction (PubMed : 11743028). Together with RNF135, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed : 28469175). Together with ZNF598, catalyzes ubiquitination of 40S ribosomal proteins in response to ribosome collisions (PubMed : 28685749). In cooperation with the GATOR2 complex, catalyzes 'Lys-6'-linked ubiquitination of NPRL2 (PubMed : 36528027).

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Post-translational modifications

Phosphorylated by AURKB.

Subcellular localisation

Endosome membrane

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Product protocols

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Target data

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592, PubMed : 28322253). In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592). Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed : 20347421). Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin (PubMed : 10329681). Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin (PubMed : 10329681). Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA (PubMed : 18948756). Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase (PubMed : 18948756). Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair (PubMed : 16628214). Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus (PubMed : 18515077). In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53 (PubMed : 12646252, PubMed : 15280377). In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes (PubMed : 18508924). In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction (PubMed : 11743028). Together with RNF135, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed : 28469175). Together with ZNF598, catalyzes ubiquitination of 40S ribosomal proteins in response to ribosome collisions (PubMed : 28685749). In cooperation with the GATOR2 complex, catalyzes 'Lys-6'-linked ubiquitination of NPRL2 (PubMed : 36528027).
See full target information UBE2D3
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