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Ubiquitin Carboxyl-Terminal Esterase L3 Human Recombinant ( UCHL3 Human )
DescriptionUCHL3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230a.a.) and having a molecular mass of 28.3kDa.UCHL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietaryRecipient :
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Storage | Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze thaw cycles. |
Formulation | The UCHL3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)1mM DTT and 10% glycerol. |
Purity | Greater than 95% as determined by SDS-PAGE. |
Description | UCHL3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230a.a.) and having a molecular mass of 28.3kDa.UCHL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. |
Protein Background | Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1. |
Expression host | Escherichia Coli. |
Synonyms | Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12. |
Reagent Appearance | Sterile Filtered clear solution. |
Amino acid sequence | MGSSHHHHHH SSGLVPRGSH MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERARYLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGETSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA |
Biological Activity | Specific activity: >3,000 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at pH 8.0, at 37C. |