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The protein encoded by HEPACAM is a single-pass type I membrane protein that localizes to the cytoplasmic side of the cell membrane. Additionally we are shipping Hepatic and Glial Cell Adhesion Molecule Proteins (11) and Hepatic and Glial Cell Adhesion Molecule Kits (4) and many more products for this protein.
Showing 10 out of 49 products:
Human Polyclonal HEPACAM Primary Antibody for IF (p), IHC (p) - ABIN758651
Maes, McGill, da Silva, Abels, Lebofsky, Maria Monteiro de Araújo, Tiburcio, Veloso Alves Pereira, Willebrords, Crespo Yanguas, Farhood, Beschin, Van Ginderachter, Zaidan Dagli, Jaeschke, Cogliati et al.: Involvement of connexin43 in acetaminophen-induced liver injury. ... in Biochimica et biophysica acta 2016
In a group of Egyptian patients with megalencephalic leukoencephalopathy, novel mutations were identified in HEPACAM.
DNMT1 (show DNMT1 Antibodies) up-regulation induced by IL-6 (show IL6 Antibodies)/STAT3 (show STAT3 Antibodies) signaling was indispensable for IL-6 (show IL6 Antibodies)-mediated hepaCAM loss in renal cell carcinoma (show MOK Antibodies) (RCC (show XRCC1 Antibodies)) cell lines ACHN (show LARP6 Antibodies) and 769-P, while DNMT3b (show DNMT3B Antibodies) up-regulation was crucial for hepaCAM loss in A498.
Out of 20 patients, macrocephaly, classic MRI (show C7ORF49 Antibodies) features, motor development delay and cognitive impairment were detected in 20(100%), 20(100%), 17(85%) and 4(20%) patients, respectively. 20(100%) were clinically diagnosed with MLC. 19(95%) were genetically diagnosed with 10 novel mutations in MLC1, MLC1 and GlialCAM mutations were identified in 15 and 4 patients, respectively
HepaCAM depletion was discovered in bladder cancer tissues compared with adjacent normal tissues, and the decreased level was associated with the degradation of FoxO3 (show FOXO3 Antibodies).
HepaCAM proteins were significantly decreased in bladder carcinoma. Low hepaCAM was not statistically associated with clinicopathological characteristics of the patients. HepaCAM overexpression activated caspase 3 (show CASP3 Antibodies)/8/9, downregulated poly-ADP ribose polymerase (show PARP1 Antibodies) and p-SMAD2 (show SMAD2 Antibodies)/3, and decreased apoptosis.
The suppressive roles of HEPACAM in NSCLC.
Due to the ability to reactivate expression of hepaCAM and inhibit growth of bladder cancer cells, AZAC may represent an effective treatment for bladder cancer.
The extracellular domain of GlialCAM is necessary for cell junction targeting and for mediating interactions with itself or with MLC1 and ClC-2 (show CLCN2 Antibodies).
HepaCAM may prevent the translocation of PKCepsilon (show PRKCE Antibodies) from cytosolic to particulate fractions, resulting in the inhibition of 786-0 cell proliferation.
GlialCAM is able to interact with all CLC (show CLC Antibodies) channels tested in this study, targeting them to cell junctions and activating them by stabilizing the open configuration of the common gate
we demonstrate an evolutionary conserved role for MLC1 in regulating glial surface levels of GLIALCAM, and this interrelationship explains why patients with mutations in either gene (MLC1 or GLIALCAM) share the same clinical phenotype.
Data indicate that membrane protein MLC1 is crucial for proper localization of adhesion molecule (show NCAM1 Antibodies) GlialCAM and chloride channel (show CLCA1 Antibodies) ClC-2 (show CLCN2 Antibodies), and for changing ClC-2 (show CLCN2 Antibodies) currents.
GlialCAM, an immunoglobulin-like cell adhesion molecule (show MCAM Antibodies) is expressed in glial cells of the central nervous system.
The protein encoded by this gene is a single-pass type I membrane protein that localizes to the cytoplasmic side of the cell membrane. The encoded protein acts as a homodimer and is involved in cell motility and cell-matrix interactions. The expression of this gene is downregulated or undetectable in many cancer cell lines, so this may be a tumor suppressor gene.
hepatocyte cell adhesion molecule
, protein hepaCAM