Recombinant Human Ubiquitin Carboxyl-Terminal Hydrolase 6 (USP6) Protein (His-KSI)

Name: Recombinant Human Ubiquitin Carboxyl-Terminal Hydrolase 6 (USP6) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-01022P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ubiquitin Carboxyl-Terminal Hydrolase 6 (USP6) Protein (His-KSI) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P35125
Target Symbol	USP6
Synonyms	(Deubiquitinating enzyme 6)(Proto-oncogene TRE-2)(Ubiquitin thioesterase 6)(Ubiquitin-specific-processing protease 6)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	KLTRKQGDLPPPAKREQGSLAPRPVPASRGGKTLCKGYRQAPPGPPAQFQRPICSASPPWASRFSTPCPGGAVREDTYPVGTQGVPSLALAQGGPQGSWRFLEWKSMPRLPTDLDIGGPWFPHYDFEWSCWVRAISQEDQLATCWQAEHCGEVHNKDMSWPEEMSFTANSSKIDRQKVPTEKGATGLS
Expression Range	348-535aa
Protein Length	Partial
Mol. Weight	36.0 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	Deubiquitinase with an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety. Catalyzes its own deubiquitination. In vitro, isoform 2, but not isoform 3, shows deubiquitinating activity. Promotes plasma membrane localization of ARF6 and selectively regulates ARF6-dependent endocytic protein trafficking. Is able to initiate tumorigenesis by inducing the production of matrix metalloproteinases following NF-kappa-B activation.
Subcellular Location	Cell membrane. Cytoplasm. Endosome. Note=Localizes to the plasma membrane and to filamentous structures within the cell corresponding to ARF6 regulated tubular endosomes. Activation of RAC1 and CDC42 can direct the relocalization of USP6 to the plasma membrane in a manner that depends on the integrity of the actin cytoskeleton.
Protein Families	Peptidase C19 family
Database References	HGNC: 12629 OMIM: 604334 KEGG: hsa:9098 STRING: 9606.ENSP00000250066 UniGene: PMID: 29617048 we identified seven novel fusion partners for USP6 in nodular fasciitis, highlighting the importance of USP6 expression and promoter-swapping fusions in the etiology of this neoplasm PMID: 28752842 Report the presence of USP6 rearrangements in a subset of cellular fibroma of tendon sheath. PMID: 27125357 our studies highlight Jak1 as the first identified substrate for USP6, and they offer a mechanistic rationale for the clinical investigation of Jak and STAT3 inhibitors as therapeutics for the treatment of bone and soft tissue tumors along with other neoplasms driven by USP6 overexpression PMID: 27440725 Molecular analyses revealed the presence and amplification of the novel PPPR6-USP6 gene fusion, which resulted in USP6 mRNA transcriptional upregulation. These findings further support the oncogenic role of the USP6 protease in mesenchymal neoplasia and expand the biologic potential of Nodular fasciitis PMID: 27113271 It was shown that TRE17 activates the classical NF-kappa B pathway through an atypical mechanism that does not involve IkappaB degradation. Optimal activation of NF-kappa B by TRE17 required both catalytic subunits of IkappaB kinase. PMID: 22081069 USP6 fluorescence in-situ hybridization is a useful ancillary test in cases where nodular fasciitis is a potential diagnostic consideration. PMID: 27271298 the deubiquitylase ubiquitin-specific protease 6 (USP6) as a potent activator of Wnt signaling. USP6 enhances Wnt signaling by deubiquitylating Fzds, thereby increasing their cell-surface abundance. PMID: 27162353 TRE17/USP6 regulates ubiquitylation and trafficking of cargo proteins that enter cells by clathrin-independent endocytosis PMID: 25179595 8 of the 9 giant cell reparative granulomas from hands and feet showed rearrangements of the USP6 gene compared with none of 8 gnathic lesions PMID: 24742829 we discuss the clinicopathologic features, molecular pathology, and pathogenesis of ABC and nodular fasciitis in relation to USP6 PMID: 23769422 identification of a USP6 gene rearrangement is helpful in making a diagnosis of nodular fasciitis. PMID: 23748914 manipulating USP6 expression levels alters the ability of cells to migrate and to divide. Cell proliferation and progression through cytokinesis depend on USP6 expression PMID: 22188517 TRE17 is sufficient to initiate tumorigenesis, identify MMPs as novel TRE17 effectors that likely contribute to aneurysmal bone cyst pathogenesis. PMID: 20418905 TRE17 coprecipitated specifically with the active forms of Cdc42 and Rac1 in vivo. TRE17 is part of a novel effector complex for Cdc42 and Rac1, potentially contributing to their effects on actin remodeling. PMID: 12612085 Complementation tests in yeasts indicate that Tre2 codes for a nonfunctional RabGAP. PMID: 14521938 Deregulated USP6 transcription is associated with aneurysmal bone cyst PMID: 15026324 primary aneurysmal bone cysts are mesenchymal neoplasms exhibiting USP6 and/or CDH11 oncogenic rearrangements PMID: 15509545 TRE17 associates directly with Arf6 in its GDP- but not GTP-bound state. PMID: 15509780 Tre2 oncogene seems to encode a nonfunctional Rab GAP. As regions flanking the TBC domain may be crucial for catalytic activity PMID: 16099424 Ca2+/CaM has a role in regulating ubiquitination through direct interaction with TRE17 PMID: 16127172 The lack of secondary structure of the region flanking the TBC domain in TRE2 may explain why this region plays a role in the lack of GAP activity, even when a potentially functional TBC domain is present. PMID: 17701273 No USP6 rearrangements were found in cherubism or brown tumors. USP6 rearrangements were identified in 2 patients with myositis ossificans. PMID: 18265974

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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.