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The protein encoded by SDCBP was initially identified as a molecule linking syndecan-mediated signaling to the cytoskeleton. Additionally we are shipping SDCBP Antibodies (126) and SDCBP Proteins (17) and many more products for this protein.
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These findings demonstrate that syntenin promotes VEGF (show VEGFA ELISA Kits) signaling and, through its PDZ-dependent interaction with ephrin-B2 (show EFNB2 ELISA Kits), enhances VEGF (show VEGFA ELISA Kits)-mediated VEGFR2 (show KDR ELISA Kits) endocytosis and subsequent downstream signaling and angiogenesis in endothelial cells
Syntenin-1 promotes invasion and progression of squamous cell carcinomas of the head and neck.
MDA-9 upregulated active levels of known modulators of epithelial mesenchymal transformation, the small GTPases RhoA (show RHOA ELISA Kits) and Cdc42 (show CDC42 ELISA Kits), via TGFbeta1 (show TGFB1 ELISA Kits), promoting lung metastasis of breast cancer cells.
a unique function of MDA-9 as a facilitator and determinant of glioma stemness and survival.
SDCBP might be an important marker for identifying Triple negative breast cancer cases that are suitable for dasatinib therapy.
ACTB (show ACTB ELISA Kits), CDKN1B (show CDKN1B ELISA Kits), GAPDH (show GAPDH ELISA Kits), GRB2 (show GRB2 ELISA Kits), RHOA (show RHOA ELISA Kits) and SDCBP are potent reference genes in neuroendocrine tumors of the lung.
In summary, the study identifies miR (show MLXIP ELISA Kits)-216b as a regulator of SDCBP expression in breast cancer which can potentially be targeted for developing newer therapies for the effective treatment of this killer disease.
Data show that patients with high MDA-9/Syntenin and high Slug expressions were associated with poor overall survival compared to those with low expression in lung adenocarcinomas.
Data suggest that syntenin/SDCBP PDZ domains 1 and 2 recognize a broad range of peptide ligands with preferences for nectin-1 (show PVRL1 ELISA Kits), hydrophobic amino acid motifs, and cryptic internal ligands/peptide fragments.
these findings demonstrate that syntenin may act as an important positive regulator of TGF-b signaling by regulating caveolin-1 (show CAV1 ELISA Kits)-mediated internalization of TbRI; thus, providing a novel function for syntenin that is linked to cancer progression.
Present study is the first demonstration of the relevance of MDA-9/Syntenin expression in regulating inflammation and immunosuppression in the microenvironment thereby impacting tumor growth and metastasis in mouse melanoma model.
Syntenin-1 negatively regulates the intestinal immunoglobulin production and has a function to maintain the intestinal homeostasis in vivo.
ALCAM (show ALCAM ELISA Kits) stably interacts with actin by binding to syntenin-1 and ezrin (show EZR ELISA Kits).
Angiopoietin-2 (show ANGPT2 ELISA Kits) secretion by endothelial cell exosomes: regulation by the phosphatidylinositol 3-kinase (PI3K)/Akt (show AKT1 ELISA Kits)/endothelial nitric oxide synthase (eNOS (show NOS3 ELISA Kits)) and syndecan-4 (show SDC4 ELISA Kits)/syntenin pathways.
MDA-9/syntenin may play a prominent role during normal mouse development in the context of cell proliferation as well as differentiation through modulating multiple signaling pathways as a crucial adaptor protein.
Complex of Unc51.1/SynGAP1/Syntenin governs axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons
Syntenin-1 may function as a scaffolding protein coupling CD6 (show CD6 ELISA Kits) and other lymphocyte receptors to cytoskeleton and/or signaling effectors during immunologic synapse maturation
syntenin plays a role in the migration of oligodendroglial precursors, and we suggest that NG2 (show Vcan ELISA Kits)-syntenin-1 interactions contribute to this
The protein encoded by this gene was initially identified as a molecule linking syndecan-mediated signaling to the cytoskeleton. The syntenin protein contains tandemly repeated PDZ domains that bind the cytoplasmic, C-terminal domains of a variety of transmembrane proteins. This protein may also affect cytoskeletal-membrane organization, cell adhesion, protein trafficking, and the activation of transcription factors. The protein is primarily localized to membrane-associated adherens junctions and focal adhesions but is also found at the endoplasmic reticulum and nucleus. Alternative splicing results in multiple transcript variants encoding different isoforms.
melanoma differentiation associated protein-9
, melanoma differentiation-associated protein 9
, pro-TGF-alpha cytoplasmic domain-interacting protein 18
, scaffold protein Pbp1
, syndecan-binding protein 1
, syndecan interacting protein
, syndecan binding protein