CYLD Antibodies

Ubiquitin carboxyl-terminal hydrolase CYLD (CYLD)

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 (PubMed:18636086, PubMed:26670046, PubMed:27458237, PubMed:26997266, PubMed:27591049, PubMed:29291351, PubMed:18313383). Plays an essential role in the regulation of pathways resulting in NF-kappa-B activation (PubMed:12917689, PubMed:12917691).

Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:18222923, PubMed:20194890).

Gene Information

Human
Gene Name:	CYLD
Uniprot:	Q9NQC7
Entrez:	1540

Family

Belongs to:
peptidase C19 family

Alternative Names

BRSS; CDMT; CYLD; CYLD1; CYLD1MFT; CYLDI; cylindromatosis (turban tumor syndrome); Deubiquitinating enzyme CYLD; EAC; EC 3.1.2.15; EC 3.4.19.12; FLJ20180; FLJ31664; KIAA0849FLJ78684; MFT1; probable ubiquitin carboxyl-terminal hydrolase CYLD; SBS; TEM; ubiquitin carboxyl-terminal hydrolase CYLD; ubiquitin specific peptidase like 2; ubiquitin thioesterase CYLD; Ubiquitin thiolesterase CYLD; Ubiquitin-specific-processing protease CYLD; USPL2

Molecular Weight

Mass (kDA):
107.316 kDA

Genomic Context

Human
Location:	16q12.1
Sequence:	16; NC_000016.10 (50742026..50801935)

Tissue Specificity

Detected in fetal brain, testis, and skeletal muscle, and at a lower level in adult brain, leukocytes, liver, heart, kidney, spleen, ovary and lung. Isoform 2 is found in all tissues except kidney.

Subcellular Localizations

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. Detected at the microtubule cytoskeleton during interphase. Detected at the midbody during telophase. During metaphase, it remains localized to the centrosome but is also present along the spindle (PubMed:25134987).

Diseases

• Neoplasms
• Skin Neoplasms
• Adenoid Cystic Carcinoma
• Ancell-spiegler Cylindromas
• Malignant Neoplasms
• Inflammation
• Trichoepithelioma
• Cell Transformation, Neoplastic
• Carcinoma
• Carcinoma, Skin Appendage
• Malignant Paraganglionic Neoplasm
• Eccrine Dermal Cylindroma

• Neoplastic Syndromes, Hereditary
• Basal Cell Carcinoma
• Infective Disorder
• Neoplasms, Multiple Primary
• Basal Cell Neoplasm
• Spiradenoma
• Benign Neoplasm

Interacting Proteins

• DDX58
• HDAC6
• ITCH
• TUBA1A

Pathways

• Pathogenesis
• Cell Death
• Cell Proliferation
• Oncogenesis
• Immune Response
• Cell Activation
• Inflammatory Response
• Cell Development
• Rna Interference
• Cell Migration
• Necroptosis
• Cell Cycle
• Localization

• Cell Growth
• Angiogenesis
• Spermatogenesis
• Osteoclast Differentiation
• Virulence
• Innate Immune Response
• Mitosis

PTMs

• Ubiquitination
• Phosphorylation
• Cleavage
• Acetylation

• Methylation
• Demethylation
• Reduction
• Deacetylation

• Dephosphorylation

Research Areas

• Cancer
• Cell Cycle and Replication

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/CYLD

Best Uses of the CYLD Marker

High-affinity primary antibodies have been the gold standard in antibody research. But how do you determine what antibodies are best for you? Here's an overview of Steven Boster's background. If you have any questions regarding CYLD Marker, read on! We'll discuss the history of this marker and the ways to use it to conduct research. Here's what you should be aware of regarding CYLD markers, as well as Boster's antibodies.

High-affinity primary antibodies

The CYLD antibodies are beneficial in immunocytochemistry, immunofluorescence and Western Blot because they recognize GPC3 on cells' surfaces. The molecular weight of the observed protein is the same as the one predicted, but could differ slightly due to post-translational modifications, cleavages, or other experimental variables. Thus, high-affinity antibody using the CYLD marker are very suitable for various applications.

The CYLD gene causes a variety of illnesses that include cylindromatosis as well as multiple trichoepitheliomas in the family, and Brook-Spiegler syndrome. This gene is affected in some individuals, which can cause a wide range of manifestations of disease. High-affinity primary antibodies made with CYLD markers were developed to detect specific antigens under these conditions and give highly reproducible and sensitive results.

A resin bead system has a tubular container that stores the sample. Each bead is coated with an antigen and immobilized onto the beads. A buffering reagent is added to improve the antigen-antibody interaction. The antibody and the antigen react to create an "antigen-antibody" complex. The antigen-antibody compound will be visualized by the secondary antibody.

The next step is to add NbALFA which is bound to the CRYLD marker to the sample. The sample was incubated at RT for 1 hour at five micrograms/mL. Then, the sample was washed three times with PBS. After that, DAPI-labelled cells were placed on glass slides using Mowiol solution. The cells were then dried at 37°C. After drying the cells were stained with FluoTag(r),-X2 or FluoTag(r) Atto488 nanobodies.

The affinity of a particular antibody is defined by the equilibrium dissociation constant (KD) which can be used to measure bimolecular interactions. It is a reversible mechanism, and the rate that an antibody binds to another is proportional with the concentrations of the reactants. The rate of dissociation is equal to the rate at which reactants break apart. KD can be measured using the constants of reaction rate. The lower the KD value, the greater affinity the antibody has towards the antigen.

The CYLD-tagged human CD62L nanobody is a highly selective antigen. The CYLD-tagged antibodies are able to detect individual members of a protein family. The antibodies can also be used to detect diseases and test for CAR-T cell development. This research has opened up a new avenue of immunological discovery. Once you've learned how to use the CYLD-tagged anti-human CD62L antibodies, you'll have an excellent foundation for developing new diagnostic tests and treatments.

Prior to that, FLAG(r)-tagged proteins were employed to detect immunostaining. Their size and complexity of expression within cells made them unsuitable for immunostaining. In addition, the HA-tagged proteins was broken down by caspases inside mammalian cells. It was therefore impossible to utilize the HA tag protein for intracellular applications.

Marker CYLD

The regulation of CYLD is extremely complex, and has been discovered to be highly controlled at both the protein and transcript levels. Multiple pathways activate CYLD and the protein interacts directly with key regulators of necrosis or development. It is crucial to understand these pathways to create new treatments for a variety of conditions. Listed below are the Best Uses of the CYLD marker. The CYLD marker is found in many tissues.

CYLD is associated with various illnesses and cellular cycles. One of these diseases is cardiovascular disease. There is increasing evidence that CYLD could be involved in blood vessel lesions. Further research is needed to better understand the role CYLD plays in vascular disease. It is essential to know how the gene is expressed in various tissues and how it is regulated. Here are a few of our favorite applications of the CYLD Marker.

The CYLD gene gives instructions for making the enzyme CYLD. Multiple signaling pathways are affected by CYLD enzyme. These pathways are vital in the development and growth of cells. It is involved in the production of various proteins that regulate activity of the Wnt, c-Jun N-terminal kinase (JNK), and Notch signaling pathways. It could be helpful in discovering the mechanisms that govern the formation of lesion.

CYLD has been shown to negatively regulate TLR2 by TRAF6 and TRAF7. It is a negative regulator of the immune system by blocking the NF-kB-dependent activation by PAMP in a mouse model of co-infection. It is easy to see how CYLD regulates lung inflammation in H. flu. This negative regulation leads to significant damage to lung tissue.

The results of this study have significant therapeutic implications for the future. The impact of in vivo CYLD on prognosis for cancer offers insight into possible targeting treatments. Further research is needed to confirm that this gene is involved in the NF-kB pathway. These findings are a step forward in the right direction for the development of new treatments for cancer. CYLD has been identified as an important protein that could be used to create new treatments.

History of Steven Boster

If you're looking for information about Steve Boster, you've come to the right place. You can find out Steve Boster's address of present and past addresses, as well as contact information and more using public records. You can also search for Steve's relatives as well as his email address. These records can be searched by state or age to gain more details. Then, you can choose to see only the public records that pertain to Steve Boster.

Steve Boster was born on July 8, 1945 in Joliet, IL. He was the son and daughter of Evelyn Meier Boster and worked in the retail industry for many years. He served in the U.S. Army and was a member of Concordia Hall in Staunton. His survivors include two daughters, Crystal Boster and Natosha Peck as well as six grandchildren, four brothers Jack Boster and Sandra Blanton and many nieces and nephews as well as great-grandchildren.