anti-UCHL1, mAb (AF3F8)

CHF 315.00
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YIF-LF-MA0319100 µlCHF 315.00
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Product Details
Synonyms UCHL1; PGP9.5; UCH-L1; PGP 9.5; EC=; Ubiquitin Thioesterase L1; Neuron Cytoplasmic Protein 9.5; Ubiquitin Carboxyl-terminal Hydrolase Isozyme L1
Product Type Monoclonal Antibody
Clone AF3F8
Isotype Mouse IgG1 κ
Immunogen/Antigen Recombinant human GST-UCHL1 protein purified from E. coli.

Western Blot (1:500~2,000)

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Isotype Negative Control

Mouse IgG1 Isotype Control

Other Product Data

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Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
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Product Specification Sheet
Datasheet Download PDF

Ubiquitin carboxy-terminal h d l L1 hydrolase (UCHL1) is a deubiqutinating enzyme. Ubiquitin UCHL1, also known as PGP9.5, is a protein of 223 amino acids and one of the most abundant proteins in the brain (1-2% of the total soluble protein). Although it was originally characterized as a deubiquitinating enzyme recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. A large amount of mono-Ub is tightly associated with UCHL1, inhibiting the degradation of mono-Ub in the brain. The precise regulation of UCHL1 is essential for neurons to survive and to maintain their proper function. UCHL1 is involved in the pathogenesis of Parkinson's disease (PD) and Alzheimer's disease (AD). Down-regulation and extensive oxidative modification of UCHL1 have been observed in the brains of AD patients as well as PD patients. A post-translational modification of UCHL1 that controls the function of UCHL1 is mono-ubiquitination. It occurs reversibly to a lysine residue near the active site of UCHL1. Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity.

Product References

1) Setsuie Rand Wada K, (2007) Neurochem Int 51(2-4):105-111. (General)
2) Gong B and Leznik E, (2007) Drug News Perspect 20(6):365-370. (General)
3) Betarbet R et al., (2005) Exp Neurol 191 Suppl 1:S17-27. (General)

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