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- Table of Contents
1 Citations 16 Q&As
1 Citations 16 Q&As
Facts about Disintegrin and metalloproteinase domain-containing protein 10.
Cleaves the membrane-bound precursor of TNF-alpha at'76-Ala-
.Human | |
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Gene Name: | ADAM10 |
Uniprot: | O14672 |
Entrez: | 102 |
Belongs to: |
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No superfamily |
a disintegrin and metalloprotease domain 10; a disintegrin and metalloproteinase domain 10; AD10; ADAM 10; ADAM metallopeptidase domain 10; ADAM10; CD156c antigen; CD156c; CDw156; disintegrin and metalloproteinase domain-containing protein 10; EC 3.4.24; HsT18717; kuz; Kuzbanian protein homolog; Kuzbanian; MADM; MADMEC 3.4.24.81; Mammalian disintegrin-metalloprotease
Mass (kDA):
84.142 kDA
Human | |
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Location: | 15q21.3 |
Sequence: | 15; NC_000015.10 (58588809..58749707, complement) |
Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver.
Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, clathrin-coated vesicle. Cell projection, axon. Cell projection, dendrite. Cell junction, adherens junction. Cytoplasm. Is localized in the plasma membrane but is also expressed in the Golgi apparatus and in clathrin-coated vesicles derived likely from the Golgi (PubMed:12475894). During long term depression, it is recruited to the cell membrane by DLG1 (PubMed:23676497). The immature form is mainly located near cytoplasmic fibrillar structures, while the matu
The ADAM10 protein is expressed in Baculovirus and is characterized by its sequence domain of 214-672 aa. It is suitable for SDS-PAGE and can be stored at +2degC to +8degC for up to a week. For longer-term storage, the protein should remain at -20degC or -80degC. Avoid repeated freeze/thaw cycles. All scientists in the world are eligible for Boster awards.
In this study, we used two PCR conditions for the ADAM10 Marker. The control was the indestructible cells. We used the ADAM10 proform, which was on the cell surface, as the control. We also used the ADAM10 gene fragment to perform PCR. These conditions were optimized to detect the presence of total mature ADAM10 protein in intact cells.
Next, we used quantitative real time PCR to determine ADAM10's expression levels. We normalized these results using GAPDH. The RNeasy Kit Qiagen was used for the isolation of RNA. After quantification, we used NanoDrop by Peqlab. For the PCR, we used the SYBR Premix Ex Taq II. The primers were made for PCR reactions. We verified the correct conditions by visual inspection.
ADAM10 deficiency induces liver progenitor cell mediated regeneration. ADAM10Dhep/Dch mice have decreased liver damage. The expression of Ki67 and CD44 in liver tissue shows increased proliferation. A total increase in serum levels of ALT/ALP was also observed in ADAM10Dhep/Dch animals aged between four and fifteen weeks. The expression of ADAM10 is correlated with LPC levels in the liver.
This study also revealed that ADAM10 is required for surface protein expression. This is thought to be a physiological mechanism that removes inactive ADAM10 cells from the cell surface. The result could lead to new therapies to block ADAM10 activity. Our findings could be used as a basis for designing inhibitors that inhibit ADAM10 activity. These inhibitors inhibit ADAM10's ability to shed.
While the presence of additional substrates to ADAM10 is concerning, the existence additional molecules that activate ADAM10 presents a good opportunity for drug discovery. These cleavage compounds could also serve as companion diagnostics or surrogate markers for ADAM10 in vivo. Additionally, additional substrates might allow for the creation of substrate-selective ADAM10 activeators.
ADAM10 is a sheddase involved in the control of the levels of the neuronal protein NrCAM under basal conditions and upon neuronal stimulation. It is possible to detect ADAM10 activity by using a PCR method. Below are the PCR conditions for the ADAM10 Marker. All of these conditions are essential for the success of this assay.
After the GI treatment, the expression of ADAM10 decreased dramatically. The expression of ADAM10 was then restored after eight hours. ADAM10 was however found to be constitutively internallyized, which indicates that it has been degraded and internalized. The ikarugamycin, an ADAM10 inhibitor, prevented ADAM10's degradation after GI treatment. Interestingly, ikarugamycin a clathrin mediated inhibition inhibitor, increased ADAM10’s surface expression after GI therapy. ADAM10 is also found to undergo shedding, de novo synthesis, and is therefore constitutively internalized.
The ADAM10 Antibody for rabbits is a polyclonal antibodies that can be used in immunoprecipitation or western blot studies. The antibody was made from immunizing animals with a protein that corresponds to human ADAM10's carboxy terminus. This antibody has been shown that it recognizes this protein in both tissues and cells. It is suitable for use in western blotting and flow cytometry.
ADAM10 acts as a scaffold to signalling proteins. It interacts directly with the Notch2 receptor as well as the E-cadherin/bcatenin signaling pathways. It also cleaves adhesion protein. This suggests that it plays a role the progression of breast cancer. Cells expressing ADAM10 showed higher levels of EGFR, notch signalling, than cells that lack this protein.
The ADAM10 gene is also known as a promoter of cell migration, invasion. Both ADAM10 knockdown or inhibition of ADAM10 protein can have different effects on cell viability. It has not been shown that ADAM10 expression in cancer cells can influence the prognosis for patients with TNBC. TNBC has not been studied in detail.
Cosmosiin blocks ADAM10 expression. Cosmosiin can also inhibit ADAM10 protein expression. The levels of ADAM10 protein in cells containing cosmosiin are significantly reduced by inhibitors of ERK and PI3K. Cosmosiin inhibitors can be used to perform ADAM10 immunofluorescence tests.
ADAM10 regulates lymphocyte growth and expression. In addition, it is important for the development of lymphocytes and initiates the canonical Notch signaling pathway. Thus, a decrease in ADAM10 expression inhibits the formation of GCs and results in decreased antigen-specific IgG production. The ADAM10 defect affects both the development of primary B cells follicles as well as germinal centres.
Adnam10 siRNA is an commercially available pooled sequence. The siRNA buffer was used at a concentration of 50 to 75 nM. Addition of scrambled control SiRNA to the same cell solution was made for ADAM10 siRNA. This treatment is repeated three times to detect the presence of the protein in the cells. The cells were visualized with an enhanced-chemiluminescence system after the third wash.
The ELISA method was used to measure the ADAM10 level in 117 primary tumour extracts. The median value of 1.16 ngm-1 was obtained. Protein levels were correlated with established variables, such as tumour severity, lymph node status, ER status, HER2, or histological type. Higher-grade tumours had higher levels of ADAM10, as were younger patients.
The ADAM10 Protein is a metalloprotease and acts as an alpha-secretase. It cleaves APP and prevents generation of pathogenic Ab peptide. The presence of ADAM10 prevents amyloid disease in neurons, while its active form in Alzheimer's patients increases amyloid disease.
ADAM10 markers have many potential uses, including in the study of adipose. ADAM10, a multifunctional protease, regulates its expression at a variety of levels including transcriptional, epigenetic and translational. These levels of regulation allow cells to quickly adapt to changes in function and at different stages of maturation. Below are examples of ADAM10 Marker applications.
ADAM10 has a wide range of substrates. Many substrates have been confirmed in vivo and in primary culture. Many have been linked with a variety biologic systems, including physiology and pathophysiology as well as cancerogenesis. A recent review summarized some of the substrates of ADAM10, and newer targets are being identified. Further research is needed to examine the relationship between ADAM10 and epilepsy.
ADAM10 is also involved in many functions of the nervous system. It regulates nerve cell communication and positioning. Researchers removed ADAM10, a gene that regulates nerve cell positioning and communication, from the brain of a mouse model. This caused abnormally structured nerve cell networks. ADAM10, which is essential for normal brain growth and prevention of Alzheimer’s disease, is also essential. Future studies may also explore the effects of stimulating ADAM10 in brain tissue. They may be able to identify specific targets, such as ADAM10-containing neuropeptides, which can affect the activity of ADAM10.
Although it is difficult for researchers to predict when ADAM10 mutants will be expressed in cell cultures, they have found that ADAM10 overexpression in human cells increases betacellulin-cleavage activity. A dominant negative mutant in dynamin I also induced higher surface ADAM10 levels. The C-terminus in ADAM10 could also serve as a signaling molecule, or facilitate nuclear entry of additional proteins. The cytoskeletal anchoring process and protein trafficking are deeply intertwined with the tetraspanins.
The ADAM10 genes has many applications. ADAM10 can be used to process synaptic adhesion chemicals such as Ncadherin. Furthermore, it can cleave APPs-alpha, a protein that plays a role in neuroprotection. ADAM10-related upregulation in the nervous is associated with short-term defense. Many studies suggest that ADAM10 might be important in neuroprotection.
Although this gene is present in various tissues of mice, it is most abundant in the developing CNS. It plays multiple roles in brain development. These proteins are processed by ADAM10's expression pattern and their putative substrates. ADAM10 cannot process a particular substrate if the two proteins are expressed in the same cellular space. This means that ADAM10 must be compared to its possible substrates to determine if they are binding friends.
The ADAM10 marker is useful in identifying axon-targeting protein. The ADAM10 protein functions as a key player in synapse formation. CHL1 (ADAM10) and NCAM (ADAM10) are essential for neuroprotection as well learning and memory. They also ensure the structural integrity and neuroprotection of neurons. Interestingly, ADAM10-deficient mice have an impaired ability to detect and respond to certain drugs and are more likely to exhibit other cognitive defects.
PMID: 9305925 by Rosendahl M.S., et al. Identification and characterization of a pro-tumor necrosis factor- alpha-processing enzyme from the ADAM family of zinc metalloproteases.
PMID: 8694785 by Howard L., et al. Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types.
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