Enzymes
Product List
UBE2V2 Human
Ubiquitin-Conjugating Enzyme E2 Variant 2 Human Recombinant
UBE2W Human
Ubiquitin Conjugating Enzyme E2W Human Recombinant
This product consists of the human UBE2W protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 171 amino acids, with the UBE2W sequence spanning amino acids 1 to 151. To facilitate purification and detection, a 20 amino acid His-tag is fused to the N-terminus of the protein. The molecular weight of the UBE2W protein with the His-tag is 19.5 kDa. The protein has been purified using proprietary chromatographic techniques to ensure its high quality and purity.
UBE2Z Human
Ubiquitin Conjugating Enzyme E2Z Human Recombinant
UCHL3 Human
Ubiquitin Carboxyl-Terminal Esterase L3 Human Recombinant
UCHL3 Mouse
Ubiquitin Carboxyl-Terminal Esterase L3 Mouse Recombinant
UCHL5 Human
Ubiquitin Carboxyl-Terminal Esterase L5 Human Recombinant
UFC1 Human
Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant
NEDD8 Human
Neural Precursor Cell Expressed Developmentally Down-Regulated 8 Human Recombinant
PTPRN Human
Protein Tyrosine Phosphatase Receptor Type N Human Recombinant
Recombinant Human PTPRN, expressed in SF9 insect cells, is a glycosylated polypeptide with an estimated molecular weight of 46kDa. This protein is engineered with a 6xHis tag for purification and is purified using proprietary chromatographic methods.
Sf9 insect cells.
SAE1 Human
SUMO1 Activating Enzyme Subunit 1 Human Recombinant
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.
