Recombinant Proteins
Product List
UCHL1 Human
Ubiquitin Carboxyl-Terminal Hydrolase L1 Human Recombinant
UCHL1 Mouse
Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant
UCHL1 Mouse, Active
Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant, Active
UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 27.2kDa.
UCHL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Ubiquitin carboxy-terminal hydrolase L1 (UCHL1) is a deubiquitinating enzyme that belongs to the peptidase C12 family. It hydrolyzes small C-terminal adducts of ubiquitin to generate the ubiquitin monomer . UCHL1 is also known by several other names, including HEL-117, NDGOA, PARK5, PGP 9.5, and PGP95 .
Key Biological Properties: UCHL1 is highly specific to neurons and cells of the diffuse neuroendocrine system . It is abundantly present in all neurons, accounting for 1-2% of total brain protein . The enzyme contains a catalytic triad consisting of cysteine at position 90, aspartate at position 176, and histidine at position 161, which are responsible for its hydrolase activity .
Expression Patterns and Tissue Distribution: UCHL1 is predominantly expressed in neurons and testis/ovary . It is also highly expressed in several forms of cancer .
Primary Biological Functions: UCHL1 plays a crucial role in the regulation of several processes, including the maintenance of synaptic function, cardiac function, inflammatory response, and osteoclastogenesis . It abrogates the ubiquitination of multiple proteins, including WWTR1/TAZ, EGFR, HIF1A, and beta-site amyloid precursor protein cleaving enzyme 1/BACE1 .
Role in Immune Responses and Pathogen Recognition: UCHL1 regulates the ability of MHC I molecules to reach cross-presentation compartments competent for generating antigen-MHC I complexes, thereby playing a role in the immune response .
Mechanisms with Other Molecules and Cells: UCHL1 interacts with various molecules and cells through its deubiquitinating activity. It stabilizes mono ubiquitin, an important component of the ubiquitin proteasome system, by preventing its degradation . UCHL1 also interacts with KLF5 and stabilizes it by reducing its polyubiquitination and proteasomal degradation .
Binding Partners and Downstream Signaling Cascades: UCHL1’s interaction with KLF5 upregulates EGFR expression while downregulating ESR1 expression at both mRNA and protein levels . It also plays a role in the JAK2/STAT3 signaling pathway, which is crucial for decidualization and the modulation of decidual NK cells .
Transcriptional Regulation: The transcription of UCHL1 is regulated by TET1 and TET3, which bind to the UCHL1 promoter region, reducing methylation of associated CpG sites and enhancing UCHL1 transcription .
Post-translational Modifications: UCHL1 undergoes various post-translational modifications that regulate its activity. For example, its deubiquitinating activity is crucial for the promotion of decidualization and the modulation of decidual NK cells .
Biomedical Research: UCHL1 is extensively studied in the context of neurodegenerative disorders such as Parkinson’s disease and Alzheimer’s disease . It is also a potential therapeutic target for these diseases due to its role in stabilizing mono ubiquitin and preventing the accumulation of ubiquitinated proteins .
Diagnostic Tools: UCHL1 is used as a biomarker for various cancers, including lung adenocarcinoma . Its expression levels can improve the detection rate of clinical lung adenocarcinoma and affect drug sensitivity .
Therapeutic Strategies: UCHL1 is a potential target for therapeutic strategies aimed at treating neurodegenerative diseases and cancers. For example, targeting UCHL1 can enhance the sensitivity of tumor cells to anti-tumor drugs .
Development to Aging and Disease: UCHL1 is not essential for neuronal development but is absolutely required for the maintenance of axonal integrity . Dysfunction of UCHL1 is implicated in neurodegenerative diseases such as Parkinson’s disease and Alzheimer’s disease . It plays a significant role in the regulation of protein degradation, and its dysfunction can lead to the accumulation of ubiquitinated proteins, contributing to cell degeneration .
