CDC34 Human
Escherichia Coli.
UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Cell Division Cycle 34 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 236 amino acids and having a molecular mass of 26.7kDa.
CDC34 is purified by proprietary chromatographic techniques.
Product Specs
CDC34 is a protein involved in cell cycle regulation and DNA replication. It functions by working with E3 complexes, like SCF, to ubiquitinate and degrade specific proteins during cell division, signaling, and development. Key targets of CDC34 include proteins like B-Myb, Wee1, and others. Additionally, proteins such as p21Cip1 and cyclin E are thought to be potential targets based on their reliance on SCF for degradation. CDC34 can self-associate and undergoes phosphorylation and ubiquitination within cells. It is a valuable tool for studying ubiquitination processes in vitro.
Recombinant human CDC34, produced in E. coli bacteria, is a single polypeptide chain without glycosylation. It consists of 236 amino acids, resulting in a molecular weight of 26.7 kDa. The purification of CDC34 is achieved through specialized chromatographic methods.
CDC34 is provided in a solution with a pH of 7.0, filtered through a 0.2 µm filter. The solution contains 50mM HEPES, 10% Glycerol, 125mM NaCl, 5% Trehalose, and 1mM DTT.
For short-term storage (up to 2-4 weeks), store the vial at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
The purity is determined to be greater than 95.0% through the following methods:
(a) RP-HPLC analysis.
(b) SDS-PAGE analysis.
UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.
Escherichia Coli.
MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES.
Product Science Overview
CDC34 is a member of the ubiquitin-conjugating enzyme family and is composed of 236 amino acids, with a molecular mass of approximately 26.7 kDa . The protein has a single polypeptide chain and is characterized by two main domains: the N-terminal domain and the C-terminal domain. The N-terminal domain contains a hydrophobic α-helix, which provides stability, while the C-terminal domain is hydrophilic and contains a cysteine residue essential for its enzymatic activity .
The primary function of CDC34 is to catalyze the covalent attachment of ubiquitin to target proteins. This process, known as ubiquitination, marks proteins for degradation by the proteasome, thus regulating protein levels within the cell. CDC34 specifically catalyzes the formation of Lys-48-linked polyubiquitin chains, which are recognized by the proteasome for degradation .
CDC34 is integral to the ubiquitin-proteasome system, which controls the degradation of key regulatory proteins involved in the cell cycle. During the G1 phase, CDC34, in conjunction with the SCF (Skp, Cullin, F-box containing complex) E3 ligase complex, ubiquitinates and targets cell cycle inhibitors such as p27^Kip1 and p21^Cip1 for degradation. This degradation is necessary for the progression into the S phase, where DNA replication occurs .
Given its pivotal role in cell cycle regulation, dysregulation of CDC34 activity can lead to various diseases, including cancer. Overexpression or mutations in CDC34 have been linked to uncontrolled cell proliferation and tumorigenesis. As a result, CDC34 is considered a potential therapeutic target for cancer treatment .
Recombinant CDC34 is produced using genetic engineering techniques, typically in Escherichia coli (E. coli) expression systems. The recombinant protein is purified using chromatographic methods to ensure high purity and activity. Recombinant CDC34 is used in research to study its function, interactions, and potential as a drug target .
CDC34 has broad applications in biomedical research and drug development. It is used to investigate the mechanisms of cell cycle regulation, protein degradation, and the role of ubiquitination in various cellular processes. Additionally, CDC34 serves as a model for developing inhibitors that can modulate its activity, offering potential therapeutic strategies for diseases such as cancer .
In conclusion, CDC34 is a critical enzyme in the ubiquitin-proteasome system, with significant implications for cell cycle regulation and disease. Understanding its structure, function, and regulation provides valuable insights into cellular processes and offers potential avenues for therapeutic intervention.
