Analytical Data
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Gene name
UCHL1
- Application
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Alternative Names
UCHL1;Ubiquitin carboxyl-terminal hydrolase isozyme L1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09936
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Expression Region
2-220aa
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AA Sequence
QLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLL LFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVAN NQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQ CRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVC REFTEREQGEVRFSAVALC
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Molecular Weight
26 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
UCHL1 (Ubiquitin C-terminal hydrolase L1) is a prominent member of the ubiquitin-proteasome system, a crucial pathway for protein degradation and regulation within cells. Its role in maintaining cellular homeostasis and protein quality control has gained considerable attention, particularly in the context of neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease, where altered ubiquitination processes are implicated. UCHL1 is believed to function as a deubiquitinating enzyme, removing ubiquitin molecules from proteins, thus preventing their degradation and influencing signaling pathways. Research has shown that mutations and aberrant expression of UCHL1 are associated with increased susceptibility to neurodegeneration, making it a potential biomarker and therapeutic target. Recombinant UCHL1 protein studies are essential for elucidating its structural and functional properties, and for understanding its role in disease mechanisms. By producing UCHL1 as a recombinant protein, researchers can investigate its enzymatic activity, binding interactions, and the effects of post-translational modifications. Such studies are pivotal in designing drugs that modulate UCHL1 activity, thereby offering prospective therapeutic avenues for neurodegenerative disorders. Furthermore, the exploration of UCHL1's interactions with other ubiquitin-regulating proteins may provide insights into the intricate network of the ubiquitin-proteasome system and its implications in disease.
