Analytical Data
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Gene name
UCHL5
- Application
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Alternative Names
UCHL5；UCH37；Ubiquitin carboxyl-terminal hydrolase isozyme L5
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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
Q9Y5K5
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Expression Region
1-326aa
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AA Sequence
MTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGNSMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKFEKHFEKTLLGK
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Molecular Weight
53.4kDa
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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
Related Products
Protein Description
UCHL5 (Ubiquitin C-terminal hydrolase L5) is a deubiquitinating enzyme that plays a crucial role in the regulation of protein degradation pathways, particularly in the context of the ubiquitin-proteasome system. This enzyme is involved in the removal of ubiquitin moieties from tagged proteins, thereby influencing various cellular processes, including cell cycle regulation, DNA repair, and signal transduction. Dysregulation of UCHL5 has been implicated in several diseases, notably cancer, where altered protein degradation pathways can lead to uncontrolled cell proliferation and survival. Research has focused on characterizing the structure and function of UCHL5, as well as its interactions with other cellular proteins. Understanding its mechanism of action could provide valuable insights into novel therapeutic interventions targeting ubiquitin-mediated pathways. Additionally, UCHL5 has been identified as a potential biomarker for certain cancers, making it a point of interest in both basic and clinical research. Studies involving the recombinant expression of UCHL5 protein have enabled researchers to explore its enzymatic activity and substrate specificity in detail, contributing to the development of potent inhibitors or modulators that could enhance therapeutic strategies in cancer treatment and other pathologies associated with ubiquitin system dysregulation.
