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AB108123

Recombinant Human Cdc26 / Apc12 protein

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(1 Publication)

Recombinant Human Cdc26 / Apc12 protein is a Human Full Length protein, in the 1 to 85 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

ANAPC12, C9orf17, CDC26, Anaphase-promoting complex subunit CDC26, Anaphase-promoting complex subunit 12, Cell division cycle protein 26 homolog, APC12

1 Images
SDS-PAGE - Recombinant Human Cdc26 / Apc12 protein (AB108123)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Cdc26 / Apc12 protein (AB108123)

15% SDS-PAGE analysis of 3µg ab108123.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Q8NHZ8

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 40% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl

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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMLRRKPTRLELKLDDIEEFENIRKDLETRKKQKEDVEVVGGSDGEGAIGLSSDPKSREQMINDRIGYKPQPKPNNRSSQFGSLEF","proteinLength":"Full Length","predictedMolecularWeight":"11.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":85,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q8NHZ8","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

Cdc26 also known as Apc12 is a protein that plays a mechanical role as a subunit of the Anaphase-Promoting Complex/Cyclosome (APC/C). This protein complex is essential for cell cycle regulation especially during the transition from metaphase to anaphase. Cdc26 has a mass of approximately 90 kDa. Expression of Cdc26 occurs mainly in dividing cells indicating its involvement in processes requiring tight cell cycle control.
Biological function summary

Cdc26/Apc12 functions as a component of the APC/C which is important for ubiquitin-mediated proteolysis of cell cycle proteins. As part of this large multi-subunit complex it aids the degradation of securin and cyclins which are proteins needed for cell cycle progression. The activity of Cdc26 is necessary to ensure correct chromosome separation during mitosis making it fundamental for maintaining genomic stability.

Pathways

Cdc26 integrates into cell cycle regulatory pathways particularly in the mitotic exit and G1 maintenance. It collaborates closely with other proteins such as Cdc20 and Cdh1 which together regulate the activity of the APC/C complex. These interactions highlight its role within the ubiquitin-proteasome signaling pathway and highlight its importance in maintaining orderly progression through the cell cycle.

Cdc26 is implicated in cancer due to its critical function in cell cycle regulation and maintenance of genomic integrity. Aberrant expression or malfunction of Cdc26 may lead to uncontrolled cell division contributing to tumorigenesis. Other proteins related to Cdc26 in cancer pathways like Cyclin B1 also play significant roles in uncontrolled cell proliferation. Additionally Cdc26 has associations with genetic disorders affecting cell division further underlining its significance in healthy cellular function.
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Specifications

Form

Liquid

Additional notes

ab108123 is purified using conventional chromatography techniques.

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General info

Function

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed : 18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins : it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed : 18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed : 29033132). May recruit the E2 ubiquitin-conjugating enzymes to the complex (PubMed : 18485873).

Sequence similarities

Belongs to the CDC26 family.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed : 18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins : it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed : 18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed : 29033132). May recruit the E2 ubiquitin-conjugating enzymes to the complex (PubMed : 18485873).
See full target information CDC26
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Cells 14: PubMed39851500

2025

Modulation of Stemness and Differentiation Regulators by Valproic Acid in Medulloblastoma Neurospheres.

Applications

Unspecified application

Species

Unspecified reactive species

Natália Hogetop Freire,Alice Laschuk Herlinger,Julia Vanini,Matheus Dalmolin,Marcelo A C Fernandes,Carolina Nör,Vijay Ramaswamy,Caroline Brunetto de Farias,André Tesainer Brunetto,Algemir Lunardi Brunetto,Lauro José Gregianin,Mariane da Cunha Jaeger,Michael D Taylor,Rafael Roesler
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