ARG70866

Human UCHL1 / PGP9.5 recombinant protein (His-tagged, C-ter)

Human UCHL1 / PGP9.5 recombinant protein (His-tagged, C-ter) for SDS-PAGE

Overview

Product Description E. coli expressed, His-tagged (C-ter) UCHL1 / PGP9.5 recombinant protein
Tested Application SDS-PAGE
Target Name UCHL1 / PGP9.5
Species Human
A.A. Sequence Gly111 - Gly210
Expression System E. coli
Alternate Names PGP95; UCH-L1; PGP9.5; PARK5; Ubiquitin thioesterase L1; HEL-117; Neuron cytoplasmic protein 9.5; Uch-L1; PGP 9.5; Ubiquitin carboxyl-terminal hydrolase isozyme L1; NDGOA; EC 3.4.19.12

Properties

Form Powder
Buffer PBS
Reconstitution It is recommended to reconstitute the lyophilized protein in sterile water to a concentration approximately 1 mg/mL and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely.
Storage Instruction For long term, lyophilized protein should be stored at -20°C or -80°C, protected from light and moisture, for up to 12 months. After reconstitution , aliquot and store at 2 to 8°C for up to 2 days, or at -20°C or -80°C for up to 3 months Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening.

Bioinformation

Gene Symbol UCHL1
Gene Full Name ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase)
Background The protein encoded by this gene belongs to the peptidase C12 family. This enzyme is a thiol protease that hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. This gene is specifically expressed in the neurons and in cells of the diffuse neuroendocrine system. Mutations in this gene may be associated with Parkinson disease.[provided by RefSeq, Sep 2009]
Function 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. [UniProt]
PTM O-glycosylated. [UniProt]