UCHL1 Human

Ubiquitin Carboxyl-Terminal Hydrolase L1 Human Recombinant
Cat. No.
BT23469
Source
Escherichia Coli.
Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, EC 3.4.19.12, Ubiquitin thioesterase L1, Neuron cytoplasmic protein 9.5, PGP 9.5, UCHL1, PGP9.5, PARK5.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

UCHL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 223 amino acids (1-223 a.a.) and having a molecular mass of 24.8 kDa (molecular weight on SDS-PAGE will appear higher).

Product Specs

Introduction
UCHL1 (PGP9.5), also known as Protein Gene Product 9.5, is a member of a gene family responsible for hydrolyzing small C-terminal adducts of ubiquitin, leading to the production of ubiquitin monomers. This protein is particularly abundant in neurons and neuroendocrine cells, playing a crucial role in these cell types. Notably, UCHL1 possesses a complex knotted structure, a characteristic believed to enhance its resistance to degradation within the cellular machinery known as the proteasome. Mutations and polymorphisms in the UCHL1 gene have been linked to neurological disorders. Specifically, the I93M mutation has been associated with Parkinson's disease in certain families, while the S18Y polymorphism appears to offer a protective effect against the same disease. Additionally, research suggests a connection between UCHL1 and Alzheimer's disease, highlighting its significance in maintaining healthy synaptic function and cognitive abilities.
Description
This product consists of the recombinant human UCHL1 protein, produced in E. coli bacteria. It is a single polypeptide chain that lacks glycosylation modifications. The chain comprises 223 amino acids (spanning positions 1 to 223) and has a molecular mass of 24.8 kDa. It's important to note that the protein's molecular weight may appear higher when analyzed using SDS-PAGE.
Physical Appearance
The product appears as a clear solution that has undergone sterile filtration.
Formulation
The UCHL1 protein is supplied in a solution with a concentration of 1 mg/ml. The solution is buffered with 20mM Tris-HCl at pH 8.0 and contains 2mM EDTA.
Stability
For short-term storage (up to 4 weeks), the product can be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein such as HSA or BSA to a final concentration of 0.1%. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of this product exceeds 95.0%, as determined by SDS-PAGE analysis.
Biological Activity

The specific activity of this product is greater than 150 pmole/min/ug. This value represents the enzyme's efficiency in hydrolyzing Ubiquitin-AMC at a pH of 8.0 and a temperature of 37°C.

Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, EC 3.4.19.12, Ubiquitin thioesterase L1, Neuron cytoplasmic protein 9.5, PGP 9.5, UCHL1, PGP9.5, PARK5.
Source
Escherichia Coli.
Amino Acid Sequence
MQLKPMEINP EMLNKVLSRL GVAGQWRFVD VLGLEEESLG SVPAPACALL LLFPLTAQHE NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLGFED GSVLKQFLSE TEKMSPEDRA KCFEKNEAIQ AAHDAVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP FPVNHGASSE DTLLKDAAKV CREFTEREQG EVRFSAVALC KAA.

Product Science Overview

Structure and Function

UCHL1 is the smallest member of the UCH family of DUBs. It catalyzes the hydrolysis of small C-terminal adducts of ubiquitin to generate ubiquitin monomers . The protein is highly specific to neurons and cells of the diffuse neuroendocrine system and their tumors . UCHL1 is predominantly expressed in the brain, where it constitutes up to 5% of the soluble protein .

Role in Neurodegenerative Diseases

Mutations in the UCHL1 gene have been associated with several neurodegenerative disorders, including Parkinson’s disease (PD). These mutations can influence the enzyme’s catalytic activity and its tendency to aggregate . UCHL1 interacts with various proteins related to the development of PD, such as alpha-synuclein, amyloid-beta precursor protein, ubiquitin-protein ligase parkin, and heat shock proteins . The balance between UCHL1’s canonical catalytic activity and its numerous activity-independent protein-protein interactions is crucial for its role in PD .

Evolutionary Perspective

The UCHL1 gene originated in early gnathostome evolutionary history and has been under strong purifying selection . A critical protein segment spanning amino acid residues 32 to 39 within the secretion site plays a significant role in protein stability, proper conformation, and interaction sites . This segment is crucial for understanding the pathogenesis of PD and offers a potential therapeutic target .

Clinical and Research Applications

UCHL1 is not only a marker for neuronal injury but also has potential implications in cancer research. It is involved in regulating cell differentiation, proliferation, and transcriptional regulation . The recombinant form of UCHL1 is used in various research applications to study its role in neurodegenerative diseases and other biological processes.

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