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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 (132) and SDCBP Kits (7) and many more products for this protein.
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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 Proteins) and Cdc42 (show CDC42 Proteins), via TGFbeta1 (show TGFB1 Proteins), 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 Proteins), CDKN1B (show CDKN1B Proteins), GAPDH (show GAPDH Proteins), GRB2 (show GRB2 Proteins), RHOA (show RHOA Proteins) and SDCBP are potent reference genes in neuroendocrine tumors of the lung.
In summary, the study identifies miR (show MLXIP Proteins)-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 Proteins), 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 Proteins)-mediated internalization of TbRI; thus, providing a novel function for syntenin that is linked to cancer progression.
To predict mda-9's association with extracellular matrix organization.
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 Proteins) stably interacts with actin by binding to syntenin-1 and ezrin (show EZR Proteins).
Angiopoietin-2 (show ANGPT2 Proteins) secretion by endothelial cell exosomes: regulation by the phosphatidylinositol 3-kinase (PI3K)/Akt (show AKT1 Proteins)/endothelial nitric oxide synthase (eNOS (show NOS3 Proteins)) and syndecan-4 (show SDC4 Proteins)/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 (show ULK1 Proteins)/SynGAP1 (show SYNGAP1 Proteins)/Syntenin governs axon formation via Ras-like GTPase signaling and through regulation of the Rab5 (show RAB5A Proteins)-mediated endocytic pathways within developing axons
Syntenin-1 may function as a scaffolding protein coupling CD6 (show CD6 Proteins) 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 Proteins)-syntenin-1 interactions contribute to this
findings show that epiboly relies on the molecular networking of syntenin with syndecan (show SDC1 Proteins) heparan sulphate proteoglycans, which act as co-receptors for adhesion molecules and growth factors
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