Recombinant Human UCHL5 Protein

Name: Recombinant Human UCHL5 Protein
Brand: Beta LifeScience
SKU: BL-0127SG
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NM_001199261
Synonym	UCH-L5, UCH37, CGI-70, INO80R
Background	UCHL5 (Ubiquitin carboxyl-terminal hydrolase isozyme L5) is a member of the peptidase C12 family of deubiquitinating enzymes and specially cleaves 'Lys-48'-linked polyubiquitin chains. UCHL5 is associated with the 19S regulatory subunit of the 26S proteasome and may play a role as a putative regulatory component of the INO80 complex (1). High expression of UCHL5 has also been indicated to be correlated with increased disease-specific survival in lymph-node-positive rectal cancer, suggesting that it could be a possible novel prognostic marker (2).
Description	Recombinant full length human UCHL5, was produced in E. coli system, fused with a His tag at N-terminus. This protein is purified with our unique purification methods.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	38 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human UCHL5 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1.
Subcellular Location	Cytoplasm. Nucleus. Note=Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus.
Protein Families	Peptidase C12 family
Database References	HGNC: 19678 OMIM: 610667 KEGG: hsa:51377 STRING: 9606.ENSP00000356425 UniGene: Hs.145469

Gene Functions References

Our study provides a new mechanism for chromatin occupancy of Tcf7 and uncovers the physiological significance of Uch37 during early vertebrate development by regulating the Wnt/beta-catenin pathway. PMID: 28198400
Our studies provide a molecular mechanism by which UCHL5 mitigates TGFbeta-1 signaling by stabilizing Smad2/Smad3. These data indicate that UCHL5 may contribute to the pathogenesis of idiopathic pulmonary fibrosis and may be a potential therapeutic target. PMID: 27604640
Positive cytoplasmic UCHL5 tumor immunoexpression is linked to increased survival of patients with small (<5 cm) tumors (p = 0.001), disease stages I-II (p = 0.025), and age 66 years or older (p = 0.037). UCHL5 is thus a potential marker in gastric cancer with new prognostic relevance. PMID: 29474458
our report demonstrates significant value in targeting USP14/UCHL5 with VLX1570 in drug-resistant Waldenstrom macroglobulinemia (WM) and carries a high potential for clinical translation PMID: 27813535
UCHL5 is a promising novel prognostic marker in lymph-node-positive rectal cancer. Our results also advance the currently limited knowledge of biomarkers in colorectal cancer treatment. PMID: 28681694
UCHL5 expression could function as a prognostic marker in pancreatic ductal adenocarcinoma, particularly at disease stages IIB to III. As UCHL5 is one of the few markers predicting increased survival, our results may be of clinical relevance. PMID: 28653876
These results uncover a novel mechanism for E2F1 transcriptional activation through removal of its Lys-63-linked ubiquitination by UCH37. PMID: 26396186
Uch37 consists of two domains, a globular UCH-domain and a fibrous C-terminal tail. The C-terminal residues of Uch37 are implicated in Rpn13 binding. PMID: 21953935
Data indicate that ubiquitin thioesterase L5 UCH37 (UCHL5) comprises a catalytic UCH domain followed by the four-helix (alpha8-alpha11) C-terminal domain. PMID: 25702872
High expression of UCH37 is significantly associated with epithelial ovarian cancer. PMID: 25123264
b-AP15 is an inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance. PMID: 24319254
UCH37 over-expression is associated with hepatocellular carcinoma recurrence. PMID: 23220010
UCH37 is associated with outcome and recurrence of ESCC and can be a novel predictor for poor prognosis of esophageal squamous cell carcinoma patients after curative resection. PMID: 22615012
a functional proteomic analysis was performed to screen UCH37-interacting proteins in hepatocellular carcinoma (HCC), and glucose-regulated protein 78 was identified as one interacting with UCH37 PMID: 21800051
our structures reveal conformationally dynamic parts of the enzyme that may play a role in the structural transition to the more active form. PMID: 21995438
Silencing of UCH37 in A549 cells induced apoptosis. PMID: 21287580
UCH37 interacts with Smads and regulates TGF-beta signalling. PMID: 16027725
Upregulation of UCH37 is associated with Uterine Cervical Neoplasms PMID: 16402389
In the nucleus Uch37 is also associated with the human Ino80 chromatin-remodeling complex (hINO80). PMID: 18922472
the crystal structure of the UCH37 catalytic domain (UCH-domain) was determined and compared with that of the other UCHs. PMID: 19836345

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.