Enzymes
Product List
UBE2A Human
Ubiquitin Conjugating Enzyme E2A Human Recombinant
UBE2B Human
Ubiquitin Conjugating Enzyme E2B Human Recombinant
The UE2B protein contains 6xHis tag and is purified by proprietary chromatographic techniques.
UBE2C Human
Ubiquitin Conjugating enzyme E2C Human Recombinant
The UBE2C is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
UBE2D1 Human
Ubiquitin Conjugating Enzyme E2D1 Human Recombinant
UBE2D1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-147 a.a.) and having a molecular mass of 19kDa.
UBE2D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
UBE2D2 Human
Ubiquitin Conjugating Enzyme E2D2 Human Recombinant
UBE2D2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (1-147) and having a molecular mass of 16.7kDa. The UBE2D2 is purified by proprietary chromatographic techniques.
UBE2D2 Human, His
Ubiquitin Conjugating Enzyme E2D2 Human Recombinant, His Tag
The UBE2D2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
UBE2D3 Human
Ubiquitin Conjugating Enzyme E2D3 Human Recombinant
UBE2D3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149a.a.) and having a molecular mass of 19.1kDa.
UBE2D3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
UBE2D4 Human
Ubiquitin Conjugating Enzyme E2D4 Human Recombinant
UBE2D4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
UBE2E1 Human
Ubiquitin Conjugating Enzyme E2E1 Human Recombinant
UBE2E1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
UBE2E3 Human
Ubiquitin Conjugating Enzyme E2E3 Human Recombinant
UBE2E3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Ubiquitin Conjugating Enzymes (E2 enzymes) are a family of enzymes that play a crucial role in the ubiquitination process, which is essential for protein degradation, signal transduction, and various cellular processes. These enzymes are classified based on their sequence homology and structural features into several families, including UBC, UEV, and others.
Key Biological Properties: E2 enzymes are characterized by their ability to transfer ubiquitin from an E1 activating enzyme to a substrate protein, often in conjunction with an E3 ligase. They possess a conserved catalytic core domain known as the UBC domain.
Expression Patterns: The expression of E2 enzymes varies widely among different tissues and cell types. Some E2 enzymes are ubiquitously expressed, while others show tissue-specific expression patterns.
Tissue Distribution: E2 enzymes are found in various tissues, including the brain, liver, heart, and muscles. Their distribution is often linked to the specific cellular functions they regulate.
Primary Biological Functions: The primary function of E2 enzymes is to facilitate the transfer of ubiquitin to target proteins, marking them for degradation by the proteasome. This process is vital for maintaining protein homeostasis and regulating various cellular pathways.
Role in Immune Responses: E2 enzymes are involved in the regulation of immune responses by modulating the stability and activity of key signaling proteins. They play a role in the activation and termination of immune signaling pathways.
Pathogen Recognition: E2 enzymes contribute to the recognition and elimination of pathogens by regulating the ubiquitination of proteins involved in pathogen sensing and response.
Mechanisms with Other Molecules and Cells: E2 enzymes interact with E1 activating enzymes to receive ubiquitin and then transfer it to substrate proteins in collaboration with E3 ligases. This interaction is highly specific and regulated.
Binding Partners: E2 enzymes have specific binding partners, including E1 enzymes, E3 ligases, and substrate proteins. These interactions determine the specificity and efficiency of the ubiquitination process.
Downstream Signaling Cascades: The ubiquitination of target proteins by E2 enzymes can activate or inhibit downstream signaling cascades, affecting various cellular processes such as cell cycle progression, DNA repair, and apoptosis.
Expression and Activity Control: The expression and activity of E2 enzymes are tightly regulated at multiple levels, including transcriptional and post-transcriptional mechanisms.
Transcriptional Regulation: The transcription of E2 enzyme genes is controlled by various transcription factors and signaling pathways, ensuring their expression is responsive to cellular needs.
Post-Translational Modifications: E2 enzymes themselves can be modified post-translationally, such as by phosphorylation or ubiquitination, which can alter their activity, stability, and interactions.
Biomedical Research: E2 enzymes are studied extensively in biomedical research for their roles in disease mechanisms, particularly in cancer, neurodegenerative diseases, and immune disorders.
Diagnostic Tools: The expression levels and activity of specific E2 enzymes can serve as biomarkers for certain diseases, aiding in diagnosis and prognosis.
Therapeutic Strategies: Targeting E2 enzymes with small molecules or inhibitors is being explored as a therapeutic strategy for diseases where dysregulated ubiquitination plays a key role.
Development: E2 enzymes are essential for proper development, as they regulate the degradation of proteins involved in cell differentiation and growth.
Aging: The activity of E2 enzymes can influence the aging process by affecting the turnover of damaged or misfolded proteins, which accumulate with age.
Disease: Dysregulation of E2 enzyme activity is implicated in various diseases, including cancer, neurodegenerative disorders, and immune diseases. Understanding their role in these conditions can lead to new therapeutic approaches.
