Analytical Data
-
Gene name
USP14
- Application
-
Alternative Names
USP14；TGT；Ubiquitin carboxyl-terminal hydrolase 14
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P54578
-
Expression Region
2-494aa
-
AA Sequence
PLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGG TLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAM ELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQY ITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDAN ECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEF ETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQ SPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPL MLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKY EPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFD DDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ
-
Molecular Weight
57 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
USP14 (Ubiquitin-specific protease 14) is a deubiquitinating enzyme that plays a critical role in the regulation of protein turnover and cellular homeostasis by removing ubiquitin moieties from proteasomal substrates. Its involvement in various cellular processes, including protein quality control, signal transduction, and stress responses, highlights its significance in maintaining cellular functions. Research has shown that dysregulation of USP14 is associated with several neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease, where the accumulation of misfolded or damaged proteins occurs. Understanding the functional mechanisms of USP14 may provide insights into therapeutic strategies for these conditions. The study of recombinant USP14 protein has garnered attention for its potential applications in drug discovery and the development of proteasome-modulating therapies. By investigating the structure, function, and interaction of USP14 with other cellular components, researchers aim to elucidate its role in ubiquitin-proteasome system regulation and its impact on cellular health. This involves recombinant expression and purification techniques to produce active USP14, allowing for in-depth biochemical and biophysical analyses. Therefore, the exploration of USP14 as a therapeutic target may pave the way for novel approaches in treating neurodegenerative disorders and advancing our understanding of protein homeostasis in human health.
