anti-UCHL1/3, pAb

CHF 322.00
In stock
YIF-LF-PA0197100 µlCHF 322.00
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Product Details
Synonyms UCHL1; UCH-L1; PGP9.5; PGP 9.5; EC=3.4.19.12; Ubiquitin Thioesterase L1; Neuron Cytoplasmic Protein 9.5; Ubiquitin Carboxyl-terminal Hydrolase Isozyme L1
Product Type Polyclonal Antibody
Properties
Immunogen/Antigen Recombinant human GST-UCHL1 protein purified from E. coli.
Application

Western Blot (1:2,000)

Crossreactivity Human
Mouse
Rat
Purity Detail Affinity purification.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Other Product Data

Click here for Original Manufacturer Product Datasheet
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.
Documents
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

The two ubiquitin C-terminal hydrolase (UCH) enzymes, UCHL1 and UCHL3, deubiquitinate ubiquitin-protein conjugates and control the cellular balance of ubiquitin. UCHL1 and UCHL3 are both small proteins of ~220 amino acids that share more than 40% amino acid sequence identity. UCHL3 is universally expressed in all tissues, while UCHL1 is expressed exclusively in neuronal tissue, testis and ovary. The activity of UCHL3 is more than 200 fold higher than UCHL1 when a fluorogenic ubiquitin substrate is used. UCHL1 associates with monoubiquitin and UCHL3 binds to Nedd8, ubiquitin-like protein. UCHL1 and UCHL3 play a role in the regulation of neuronal development and spermatogenesis. 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. 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) Osaka H et al., (2003) Human Molecular. (General)
2) Genetics 12(16):1945–1958. (General)
3) Kwon J, (2007) Exp Anim 56:71-7. (General)
4) Sakurai M et al., (2006) J Cell Sci 119:162-171. (General)

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