Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

Cyld

Uniprot No.

Q80TQ2

Research Area

Cancer

Species

Mus musculus (Mouse)

Source

E.coli

Expression Region

579-952aa

Target Protein Sequence

GLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDIEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

50.6 kDa

Protein Length

Partial

Tag Info

N-terminal 10xHis-tagged and C-terminal Myc-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The recombinant Mouse Cyld was expressed with the amino acid range of 579-952. This Cyld protein is expected to have a theoretical molecular weight of 50.6 kDa. The Cyld protein was expressed in e.coli. The Cyld coding gene included the N-terminal 10xHis tag and C-terminal Myc tag, which simplifies the detection and purification processes of the recombinant Cyld protein in following stages of expression and purification.

The mouse ubiquitin carboxyl-terminal hydrolase CYLD is a deubiquitinating enzyme that can remove ubiquitin chains from target proteins, thereby controlling protein stability and cellular signaling pathways. One of its main functions is to negatively regulate NF-κB signaling by deubiquitinating key components in the pathway. CYLD also influences other cellular processes such as cell cycle progression, apoptosis, and immune response. Dysregulation of CYLD has been linked to various diseases, including cancers and inflammatory disorders. Understanding the molecular functions of CYLD provides insights into its potential therapeutic applications in these conditions.

Target Background

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.

Gene References into Functions

Loss of CYLD catalytic activity causes impaired DNA damage-induced p53 stabilization and activation in epithelial cells and sensitizes mice to chemical carcinogen-induced intestinal and skin tumorigenesis. 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

Hide All

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 Links

KEGG: mmu:74256

STRING: 10090.ENSMUSP00000096119

UniGene: Mm.490395

Code	CSB-EP773899MO
Abbreviation	Recombinant Mouse Cyld protein, partial
MSDS	MSDS Datasheet
Size	$388
	Order now
Image	Warning: preg_replace(): Unknown modifier 'a' in /www/wwwroot/cusabio.com/caches/caches_template/20141113/content/show_product_protein.php on line 156
Have Questions?	Leave a Message or Start an on-line Chat

Recombinant Mouse Ubiquitin carboxyl-terminal hydrolase CYLD (Cyld), partial

Product Details

Related Products

Customer Reviews and Q&A

Target Background

×CloseMessage