Recombinant Mouse Ubiquitin Carboxyl-Terminal Hydrolase Cyld (CYLD) Protein (His&Myc)

Name: Recombinant Mouse Ubiquitin Carboxyl-Terminal Hydrolase Cyld (CYLD) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07165P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Ubiquitin Carboxyl-Terminal Hydrolase Cyld (CYLD) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q80TQ2
Target Symbol	CYLD
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	GLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDIEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
Expression Range	579-952aa
Protein Length	Partial
Mol. Weight	50.6 kDa
Research Area	Cancer
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 that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation. Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation. Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation. Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1. Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades.
Subcellular Location	Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, cilium basal body.
Protein Families	Peptidase C19 family
Database References	KEGG: mmu:74256 STRING: 10090.ENSMUSP00000096119 UniGene: PMID: 27561390 The present results support the involvement of CYLD in the regulation of NF-kappaB inflammatory signaling induced by elevated glucose, implicating CYLD as a potential therapeutic target of diabetic nephropathy . PMID: 29259980 the role of CYLD in development, tissue homeostasis, and tumorigenesis PMID: 28750888 Findings provide physiological insight into the ciliary role of the CYLD/HDAC6 axis and suggest a functional interplay between these two proteins in ciliary homeostasis. PMID: 27028867 Thrombin-mediated MALT1 protease activation triggers acute disruption of endothelial barrier integrity via CYLD cleavage. PMID: 27681433 SPATA2 has been described as a previously unrecognized factor in the linear ubiquitin chain assembly complex-dependent signaling pathways that serves as an adaptor between HOIP and CYLD, thereby enabling recruitment of CYLD to signaling complexes. PMID: 27545878 TLR4 activates CASPASE-8 to cleave and remove the deubiquitinase cylindromatosis (CYLD) in a TRIF- and RIPK1-dependent manner to disable necroptosis in macrophages. PMID: 27264187 CYLD contributes to the transdifferentiation of adventitial fibroblasts via deubiquitinating Nox4 and may play a role in vascular remodeling. PMID: 28751569 this study shows that by polarization of the T cell cytokine response, CYLD can favor the development of allergic airway disease PMID: 27372382 Our findings underscore a critical tumor-suppressing role for functional intestinal epithelial CYLD in colitis-associated carcinogenesis PMID: 27042826 Deubiquitinase CYLD negatively regulates MyD88-mediated signaling by directly interacting with MyD88 and deubiquitinating nontypeable Haemophilus influenzae (NTHi)-induced K63-linked polyubiquitination of MyD88 at lysine 231. PMID: 26719415 CYLD interrupts the ERK- and p38-/AP-1 and c-Myc pathways to suppress Nrf2-operated antioxidative capacity, thereby enhancing oxidative stress in the heart. PMID: 25935309 Our data demonstrate that inefficient negative selection in the thymus of CYLD(ex7/8) mice result from a defect in mTEC maturation. PMID: 25601276 The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells. PMID: 25134987 Data show that the in utero death of NF-NF-kappaB essential modulator (NEMO) and cylindromatosis protein double mutant mice is mediated by TNF receptor 1 (TNFR1) signaling and can be rescued by TNFR1 deficiency. PMID: 26224629 CYLD is a central regulator of apoptotic cell death in murine hepatocytes by controlling NF-kappaB dependent anti-apoptotic signaling. PMID: 25493017 In contrast to full-length CYLD, the immune function of short splice variant CYLD (sCYLD) is insufficiently described. To explore sCYLD's function in infection, investigated whether dendritic cell-specific sCYLD regulates the pathogenesis of listeriosis. PMID: 25675948 The ciliary function of CYLD is partially attributed to its deconjugation of the polyubiquitin chain from centrosomal protein of 70 kDa (Cep70), a requirement for Cep70 to interact with gamma-tubulin and localize at the centrosome. PMID: 25342559 CYLD negatively regulates nontypeable Haemophilus influenzae-induced IL-8 expression via MKP-1-dependent inhibition of ERK. PMID: 25389768 identifying the CYLD-TRAF2-p38MAPK pathway as a novel important regulator of HSC function restricting HSC cycling and promoting dormancy. PMID: 25824820 RBP-J-mediated Notch signaling is required for macrophages to promote hepatic fibrosis by up-regulation of NF-kappaB activation through CYLD. PMID: 25145286 CYLD is required for Toll-like receptor-induced necroptosis PMID: 24706750 Through regulation of hepatocyte growth factor level, CYLD ameliorates hepatocellular damage and liver fibrogenesis. PMID: 24811579 CYLD regulates RIP1 ubiquitination in the TNFalpha-induced necrosome to facilitate kinase activation and programmed necrosis. PMID: 24098568 Downregulation of CYLD induces tumor cell proliferation, consequently contributing to the aggressive growth of hepatocellular carcinoma. PMID: 24104553 fibrin production, pathogen control and survival of Lm-infected WT mice illustrating that therapeutic inhibition of CYLD augments the protective NF-kappaB/IL-6/STAT3 pathway and fibrin production. PMID: 23825949 Functional inactivation of CYLD promotes the metastatic potential of tumor epidermal cells. PMID: 23426135 PKCtheta;/beta and CYLD are antagonistic partners in the NFkappaB and NFAT transactivation pathways in primary mouse CD3+ T lymphocytes. PMID: 23335970 an essential role of CYLD in maintaining T cell homeostasis as well as normal T regulatory cell function, thereby controlling abnormal T cell responses. PMID: 23066153 loss of deubiquitinase CYLD led to the development of lung fibrosis in mice after infection with Streptococcus pneumoniae; CYLD regulates the resolution of lung injury and prevents fibrosis by deubiquitinating Akt PMID: 22491319 Results show that, in the liver, CYLD acts as an important regulator of hepatocyte homeostasis, protecting cells from spontaneous apoptosis by preventing uncontrolled TAK1 and JNK activation. PMID: 22698400 we have identified an Itch-Cyld-mediated regulatory mechanism in innate inflammatory cells. PMID: 22057290 these results uncover an unexpected role of CYLD in promoting inflammatory responses in VSMCs via a mechanism involving MAPK activation but independent of NF-kappaB activity, contributing to the pathogenesis of vascular disease. PMID: 22406061 The findings establish CYLD as a novel regulator of antiviral innate immunity and suggest a role for CYLD in regulating IFN receptor signaling. PMID: 21946435 CYLD regulates TGF-beta signaling function in T cells and the development of Tregs through deubiquitination of Smad7 PMID: 21931165 data establish CYLD as a critical regulator of thymocyte selection in a manner that depends on IKK2 and NF-kappaB activation PMID: 21728169 These results show that SRF acts as a positive regulator of CYLD expression. PMID: 21573132 Hes1 expression and CYLD repression are essential events downstream of Notch1 in T-cell leukemia. PMID: 21389783 CYLD is a regulator of monocyte-macrophage activation in response to inflammatory stimuli PMID: 21283724 Study identifies a fundamental role for functional CYLD in establishing the proper threshold of activation for thymocyte selection by a mechanism dependent on NF-kappaB essential modulator. PMID: 20644164 CYLD regulates homeostasis of immature Natural killer T cells via a novel mechanism that involves regulation of IL-7R signalling and ICOS expression. PMID: 20224552 CYLD is induced by NF-kappaB PMID: 15226292 identifed CYLD as a positive regulator of proximal T cell receptor signaling in thymocytes PMID: 16501569 These data indicate that, depending on the external signals, Cyld can negatively regulate different NF-kappaB pathways; inactivation of TRAF2 controls survival and inflammation, while inhibition of Bcl-3 controls proliferation and tumor growth. PMID: 16713561 CYLD limits inflammation and tumorigenesis by regulating ubiquitination in vivo PMID: 17053834 a critical role for CYLD in regulating the basal activity of NF-kappaB and maintaining the naive phenotype and proper activation of B cells. PMID: 17392286 CYLD plays a critical role in preventing spontaneous activation of the Tak1 axis of T cell signaling and, thereby, maintaining normal T cell function. PMID: 17548520 identifies CYLD for the first time as a critical negative regulator of host antiviral response PMID: 17608805 CYLD is detrimental for host survival, thereby indicating a mechanism underlying the high early mortality of pneumococcal pneumonia. PMID: 17723219 CYLD can both positively and negatively regulate signal transduction and homeostasis of B cells in vivo, depending on the expression of CYLD splice variants. PMID: 17923499

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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.

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