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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.
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Human Polyclonal HEPACAM Primary Antibody für 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
hepaCAM associates with connexin 43 (zeige GJA1 Antikörper), a main component of gap junctions, and enhances connexin 43 (zeige GJA1 Antikörper) localization to the plasma membrane at cellular junctions.
this study revealed that hepaCAM was downregulated in CRC (zeige CALR Antikörper) tissues and cell lines. Overexpression of hepaCAM inhibited CRC (zeige CALR Antikörper) cell proliferation, migration, and invasion in vitro. Furthermore, the tumorigenesis assay showed that increased expression of hepaCAM suppressed CRC (zeige CALR Antikörper) tumor growth and metastasis in vivo.
In a group of Egyptian patients with megalencephalic leukoencephalopathy, novel mutations were identified in HEPACAM.
DNMT1 (zeige DNMT1 Antikörper) up-regulation induced by IL-6 (zeige IL6 Antikörper)/STAT3 (zeige STAT3 Antikörper) signaling was indispensable for IL-6 (zeige IL6 Antikörper)-mediated hepaCAM loss in renal cell carcinoma (zeige MOK Antikörper) (RCC (zeige XRCC1 Antikörper)) cell lines ACHN (zeige LARP6 Antikörper) and 769-P, while DNMT3b (zeige DNMT3B Antikörper) up-regulation was crucial for hepaCAM loss in A498.
Out of 20 patients, macrocephaly, classic MRI (zeige C7ORF49 Antikörper) 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 (zeige FOXO3 Antikörper).
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 (zeige CASP3 Antikörper)/8/9, downregulated poly-ADP ribose polymerase (zeige PARP1 Antikörper) and p-SMAD2 (zeige SMAD2 Antikörper)/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 (zeige CLCN2 Antikörper).
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 (zeige NCAM1 Antikörper) GlialCAM and chloride channel (zeige CLCA1 Antikörper) ClC-2 (zeige CLCN2 Antikörper), and for changing ClC-2 (zeige CLCN2 Antikörper) currents.
GlialCAM, an immunoglobulin-like cell adhesion molecule (zeige MCAM Antikörper) 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