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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 Antibodies (57) and Hepatic and Glial Cell Adhesion Molecule Kits (7) and many more products for this protein.
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On the whole, this study indicates that HepaCAM potentially represents a therapeutic target and PF3084014 may prove to a promising agent for use in the treatment of refractory prostate cancer.
hepaCAM associates with connexin 43 (show GJA1 Proteins), a main component of gap junctions, and enhances connexin 43 (show GJA1 Proteins) localization to the plasma membrane at cellular junctions.
this study revealed that hepaCAM was downregulated in CRC (show CALR Proteins) tissues and cell lines. Overexpression of hepaCAM inhibited CRC (show CALR Proteins) cell proliferation, migration, and invasion in vitro. Furthermore, the tumorigenesis assay showed that increased expression of hepaCAM suppressed CRC (show CALR Proteins) tumor growth and metastasis in vivo.
In a group of Egyptian patients with megalencephalic leukoencephalopathy, novel mutations were identified in HEPACAM.
DNMT1 (show DNMT1 Proteins) up-regulation induced by IL-6 (show IL6 Proteins)/STAT3 (show STAT3 Proteins) signaling was indispensable for IL-6 (show IL6 Proteins)-mediated hepaCAM loss in renal cell carcinoma (show MOK Proteins) (RCC (show XRCC1 Proteins)) cell lines ACHN (show LARP6 Proteins) and 769-P, while DNMT3b (show DNMT3B Proteins) up-regulation was crucial for hepaCAM loss in A498.
Out of 20 patients, macrocephaly, classic MRI (show C7ORF49 Proteins) 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 Proteins).
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 Proteins)/8/9, downregulated poly-ADP ribose polymerase (show PARP1 Proteins) and p-SMAD2 (show SMAD2 Proteins)/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.
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 Proteins) GlialCAM and chloride channel (show CLCA1 Proteins) ClC-2 (show CLCN2 Proteins), and for changing ClC-2 (show CLCN2 Proteins) currents.
GlialCAM, an immunoglobulin-like cell adhesion molecule (show MCAM Proteins) 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