Enzymes
Product List
UCHL3 Human
Ubiquitin Carboxyl-Terminal Esterase L3 Human Recombinant
UCHL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
UCHL3 Mouse
Ubiquitin Carboxyl-Terminal Esterase L3 Mouse Recombinant
UCHL3 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
UCHL5 Human
Ubiquitin Carboxyl-Terminal Esterase L5 Human Recombinant
UCHL5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
UFC1 Human
Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant
UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.
UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NEDD8 Human
Neural Precursor Cell Expressed Developmentally Down-Regulated 8 Human Recombinant
The NEDD8 is purified by proprietary chromatographic techniques.
PTPRN Human
Protein Tyrosine Phosphatase Receptor Type N Human Recombinant
Recombinant Human Protein Tyrosine Phosphatase Receptor Type N produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa.
PTPRN is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Sf9 insect cells.
SAE1 Human
SUMO1 Activating Enzyme Subunit 1 Human Recombinant
SAE1/SAE2 Human
SAE1/SAE2 Human Recombinant
SAE1/SAE2 Human Recombinant produced in SF9 is glycosylated, polypeptide chain containing 2 subunits (SAE1 subunit molecular mass is 41kDa & SAE2 subunit molecular mass is 91kDa). The subunits associate to form a complex.
The SAE1/SAE2 is expressed with a -10xHis tag and purified by proprietary chromatographic techniques.
Sf9 insect cells.
UBA2 Human
Ubiquitin-Like Modifier Activating Enzyme 2 Human Recombinant
UBA2 Human Recombinant produced in in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 649 amino acids (1-640a.a) and having a molecular mass of 72.3kDa. UBA2 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
UBA3 Human
Ubiquitin-Like Modifier Activating Enzyme 3 Human Recombinant
UBA3 is fused to a 24 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.
