Recombinant Human Ubl Carboxyl-Terminal Hydrolase 18 (USP18) Protein (His&Myc)

Name: Recombinant Human Ubl Carboxyl-Terminal Hydrolase 18 (USP18) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06849P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Ubl Carboxyl-Terminal Hydrolase 18 (USP18) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9UMW8
Target Symbol	USP18
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MSKAFGLLRQICQSILAESSQSPADLEEKKEEDSNMKREQPRERPRAWDYPHGLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCNVPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNPNYHWQETAYLLVYMKMEC
Expression Range	1-372aa
Protein Length	Full Length
Mol. Weight	50.5 kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in the negative regulation of the inflammatory response triggered by type I interferon. Upon recruitment by STAT2 to the type I IFN receptor subunit IFNAR2 interferes with the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and acts as a negative regulator of the type I IFN signaling pathway. Also regulates protein ISGylation. Can efficiently cleave only ISG15 fusions including native ISG15 conjugates linked via isopeptide bonds. Necessary to maintain a critical cellular balance of ISG15-conjugated proteins in both healthy and stressed organisms.; Has enzymatic activity similar to isoform 1 and interferes with type I interferon signaling. Major deISGylation enzyme for nuclear proteins.
Subcellular Location	[Isoform 1]: Cytoplasm.; [Isoform 2]: Nucleus. Cytoplasm.
Protein Families	Peptidase C19 family
Database References	HGNC: 12616 OMIM: 607057 KEGG: hsa:11274 STRING: 9606.ENSP00000215794 UniGene: PMID: 28630501 The role of USP18 in breast cancer provides a novel insight into the clinical application of the USP18/AKT/Skp2 pathway. PMID: 29749454 High expression levels of USP18 in the muscles of dermatomyositis patients. PMID: 27605457 study preliminary elucidated the role of USP18 in hepatitis B virus replication and explored the potential key genes in USP18-mediated signaling pathway PMID: 28369997 this study identified PTEN as a previously unrecognized substrate of the ISGylation post-translational modification pathway. The deconjugase USP18 serves as a novel regulator of PTEN stability. This indicates inhibition of ISGylation is therapeutically relevant in cancers. PMID: 27980214 associates with and deubiquitinates TAK1 to protect against hepatic steatosis, insulin resistance, and the inflammatory response PMID: 28718215 that Ubiquitin-specific peptidase 18 directly bind to BCL2L1 and positively regulated its expression in hepatocellular carcinoma cells PMID: 28709980 These findings add USP18 deficiency to the list of genetic disorders collectively termed type I interferonopathies PMID: 27325888 We show that IRF-7 siRNA knockdown enhanced LPS-induced IL-10 production in human monocyte-derived macrophages, and USP-18 overexpression attenuated LPS-induced production of IL-10 in RAW264.7 cells. Quantitative PCR confirmed upregulation of USP18, USP41, IL10, and IRF7. An independent cohort confirmed LPS induction of USP41 and IL10 genes PMID: 27434537 results indicated that USP18 modulates the anti-HBV activity of IFN-F via activation of the JAK/STAT signaling pathway in Hepg2.2.15 cells. PMID: 27227879 USP18's ISG15 specificity is mediated by a small interaction interface. PMID: 28165509 STAT2 recruits USP18 to the type I IFN receptor subunit IFNAR2 via its constitutive membrane-distal STAT2-binding site. PMID: 28165510 findings show that multiple inflammatory stimuli can modulate interferon stimulated gene expression and thus inhibit hepatocyte interferon signaling via USP18 induction PMID: 27009955 USP18 negatively regulates NF-kappaB signaling by targeting TAK1 and NEMO for deubiquitination through distinct mechanisms. PMID: 26240016 Data suggest that USP18 (Ubiquitin-like specific protease 18) sensitive cellular functions include activity of the peptide transporters PEPT1 and PEPT2. PMID: 26046984 Dimerization of IFNAR1 and IFNAR2 and the limiting role of IFNAR1 binding affinity in complex assembly is modulated by USP18. PMID: 26008745 increased expression in the HIV+/HCV+ female patients group compared with HIV-/HCV+ and HIV+/HCV- groups PMID: 24955730 USP18 expression levels induced by IFNbeta did not differ amongst multiple sclerosis patients carrying different rs2542109 genotypes PMID: 23700969 USP18 inhibition induces inflammation by increasing the STAT signaling and exacerbates IFN-induced beta cell apoptosis. PMID: 23152055 Usp18 upregulation was associated with Wilms Tumor. PMID: 23291318 A direct relationship was found between UBP43 and cyclin D1 (but not cyclin E) expression. PMID: 22752428 USP18 establishes the transcriptional and anti-proliferative interferon alpha/beta differential PMID: 22731491 USP18 is up-regulated in liver samples of patients with chronic hepatitis C that did not respond to therapy, but not in patients with acute hepatitis C. PMID: 22677194 although UBP43 depletion can cause hypersensitivity to interferon-alpha/beta-mediated apoptosis in a broad range of cell types, the downstream pathway may vary depending on the cell type. PMID: 22683641 the existence of an N-terminal truncated isoform of USP18, whose expression is controlled on translational level by two independent mechanisms providing translational flexibility PMID: 22170061 Inhibition of R. conorii-induced ISG15 by RNA interference results in significant increase in the extent of rickettsial replication, whereas UBP43 knockdown yields a reciprocal inhibitory effect. PMID: 22100648 a model in which Usp18 inhibition promotes up-regulation of miR-7, which in turn inhibits EGFR expression and the tumorigenic activity of cancer cells. PMID: 21592959 Findings define the ubiquitin protease UBP43 as a novel candidate drug target for APL treatment. PMID: 20935222 Findings suggest that USP18 may significantly limit operation of the extrinsic apoptotic pathway triggered by type I IFN and drugs. PMID: 20068173 UBP43 protein levels are regulated by proteolysis via the SCFSkp2 ubiquitin ligase PMID: 15342634 Ubp43 deficiency increases the resistance to oncogenic transformation by BCR-ABL PMID: 17374743 Epstein-Barr virus independent dysregulation of UBP43 expression alters interferon-stimulated gene expression in Burkitt lymphoma PMID: 19551150

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.