JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB151828

Recombinant Human Cdc34 protein

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant Human Cdc34 protein is a Human Full Length protein, in the 1 to 236 aa range, expressed in Escherichia coli, with >75%, suitable for SDS-PAGE, WB.

View Alternative Names

UBCH3, UBE2R1, CDC34, Ubiquitin-conjugating enzyme E2 R1, (E3-independent) E2 ubiquitin-conjugating enzyme R1, E2 ubiquitin-conjugating enzyme R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, Ubiquitin-conjugating enzyme E2-CDC34, Ubiquitin-protein ligase R1

1 Images
SDS-PAGE - Recombinant Human Cdc34 protein (AB151828)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Cdc34 protein (AB151828)

SDS-PAGE analysis of ab151828 which was determined to be >75% pure by densitometry.

Key facts

Purity

>75% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, WB

applications

Biologically active

No

Accession

P49427

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7 Preservative: 1.02% Imidazole Constituents: 25% Glycerol (glycerin, glycerine), 1.76% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

style
left-column

Complementary Products

Proteins & Peptides

AB173055

Recombinant Human UBE2Z protein

  • 0
  • 0
Proteins & Peptides

AB167941

Recombinant Human MDM2 protein

SDS-PAGE - Recombinant Human MDM2 protein (AB167941)

  • 5
  • 1
Proteins & Peptides

AB269138

Recombinant human Wwp2 protein (Active)

Functional Studies - Recombinant human Wwp2 protein (Active) (AB269138)

  • 0
  • 0
Proteins & Peptides

AB167921

Recombinant Human UBE2W protein

SDS-PAGE - Recombinant Human UBE2W protein (AB167921)

  • 0
  • 0
style
left-column

Reactivity data

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

Sequence info

[{"sequence":"MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEEADSCFGDDEDDSGTEES","proteinLength":"Full Length","predictedMolecularWeight":"33 kDa","actualMolecularWeight":null,"aminoAcidEnd":236,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P49427","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
style
left-column

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
False
style
left-column

Supplementary information

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

The Cdc34 protein also known as Ubc3 is a ubiquitin-conjugating enzyme with a molecular mass of about 35 kDa. It is expressed in various tissues with high presence in actively dividing cells. Cdc34 plays a significant role in cell cycle regulation particularly during the transition from G1 to the S phase. It facilitates the attachment of ubiquitin molecules to target proteins marking them for degradation by the proteasome which is important for controlling the abundance of specific proteins involved in cell cycle progression.
Biological function summary

Cdc34 functions as a member of the SCF (SKP1-CUL1-F-box) ubiquitin ligase complex. This complex targets a range of key regulatory proteins for ubiquitination influencing processes such as DNA replication and repair. By mediating protein degradation Cdc34 helps regulate the cellular levels of cyclins which are essential for proper cell cycle advancement. Its activity ensures timely degradation of these cyclins thereby preventing unscheduled cell cycle transitions that can lead to cellular dysfunction.

Pathways

Cdc34 is integrated in the ubiquitin-proteasome pathway and the cell cycle pathway. In these contexts Cdc34's activity closely interacts with proteins like Skp2 another component of the SCF complex which regulates G1-S phase transition. Cdc34-related pathways ensure that protein turnover is tightly controlled which is essential for maintaining cellular homeostasis and responding to internal and external signals during cell proliferation.

Cdc34 links to cancer and neurodegenerative disorders. Alterations in Cdc34 function can result in the aberrant degradation of regulatory proteins contributing to unchecked cell proliferation a hallmark of cancer. Furthermore imbalances in ubiquitin-proteasome pathway components including Cdc34 relate to neurodegenerative diseases where protein aggregation occurs. Connections to proteins such as p27 which regulates cell cycle and accumulation issues in neurological tissues highlight the significance of Cdc34 in disease mechanisms.
style
left-column

Specifications

Form

Liquid

Additional notes

assessed by densitometry

style
left-column

General info

Function

E2 ubiquitin-conjugating enzyme that accepts ubiquitin from an E1 ubiquitin-activating protein, and catalyzes its covalent attachment to other proteins by an E3 ubiquitin-protein ligase complex (PubMed : 10329681, PubMed : 17588522, PubMed : 20061386, PubMed : 38326650). In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed : 22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed : 10329681, PubMed : 10918611, PubMed : 17698585). Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1 (PubMed : 10871850, PubMed : 15652359, PubMed : 19112177). Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation (PubMed : 19126550). Also involved in the degradation of beta-catenin (PubMed : 12037680). Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed : 11805320, PubMed : 12060736).

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Post-translational modifications

Autoubiquitinated (PubMed:11805320, PubMed:12060736, PubMed:22496338). Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway (PubMed:11805320, PubMed:12060736).. Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controls the nuclear localization.

Subcellular localisation

Nucleus

style
left-column

Product protocols

style
left-column

Target data

E2 ubiquitin-conjugating enzyme that accepts ubiquitin from an E1 ubiquitin-activating protein, and catalyzes its covalent attachment to other proteins by an E3 ubiquitin-protein ligase complex (PubMed : 10329681, PubMed : 17588522, PubMed : 20061386, PubMed : 38326650). In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed : 22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed : 10329681, PubMed : 10918611, PubMed : 17698585). Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1 (PubMed : 10871850, PubMed : 15652359, PubMed : 19112177). Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation (PubMed : 19126550). Also involved in the degradation of beta-catenin (PubMed : 12037680). Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed : 11805320, PubMed : 12060736).
See full target information CDC34
style
left-column
style
left-column
style
right-column

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com