Human UCH-L1, His Tag (UC1-H5140) is expressed from E.coli cells. It contains AA Gln 2 - Ala 223 (Accession # NP_004172).
Predicted N-terminus: Met
This protein carries a polyhistidine tag at the N-terminus.
The protein has a calculated MW of 25.7 kDa. The protein migrates as 27-28 kDa under reducing (R) condition (SDS-PAGE).
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM Nacl, pH8.0. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human UCH-L1, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCHL1) ,a member of the peptidase C12 family, is also known as neuron cytoplasmic protein 9.5 (PGP 9.5) and ubiquitin thioesterase L1.About 30% of total UCHL1 is associated with membranes in brain. UCHL1 is 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,UCHL1 can bind to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. Furthermore, the mutations of UCHL1 gene can result in parkinson disease 5.