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Human UCHL1 Protein, His tag

Human UCHL1 Protein, His tag

Catalog Number: S0A9057 Reactivity: Human Conjugation: Unconjugated Brand: Starter
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Regular price $318.00 SGD
Regular price Sale price $318.00 SGD
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Product Details

Product Specification


Species Human
Synonyms Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5 (PGP9.5), Ubiquitin thioesterase L1
Accession P09936
Amino Acid Sequence

Protein sequence (P09936, Gln2-Ala223, with N-His tag) QLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVCREFTEREQGEVRFSAVALCKAA

Expression System E.coli
Molecular Weight

Predicted MW: 26.5 kDa Observed MW: 26.5 kDa

Purity >95% by SDS-PAGE
Endotoxin <0.1EU/μg
Conjugation Unconjugated
Tag with N-His tag
Physical Appearance Lyophilized Powder
Storage Buffer Lyophilized from a 0.2 μm filtered solution of 0.2M PBS, pH7.4.
Reconstitution Reconstitute no more than 1 mg/mL according to the size in deionized water after rapid centrifugation.
Stability & Storage

12 months from date of receipt, -20 to -70 °C as supplied.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
1 week, 2 to 8 °C under sterile conditions after reconstitution.
Please avoid repeated freeze-thaw cycles.

Background

Ubiquitin carboxy-terminal hydrolase L1 (EC 3.1.2.15, ubiquitin C-terminal hydrolase, UCH-L1) is a deubiquitinating enzyme. UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. It is abundantly present in all neurons (accounts for 1-2% of total brain protein), expressed specifically in neurons and testis/ovary. The catalytic triad of UCH-L1 contains a cysteine at position 90, an aspartate at position 176, and a histidine at position 161 that are responsible for its hydrolase activity.

Picture

SDS-PAGE

2 μg(R: reducing conditions)

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