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cell+culture+plates
Numéro de catalogue:
(BOSSBS-1497R-A555)
Fournisseur:
Bioss
Description:
The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. Modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, influences directly or indirectly the Ras/MAPK pathway. Promotes tumor progression. Regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1300R-CY5)
Fournisseur:
Bioss
Description:
Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1300R-HRP)
Fournisseur:
Bioss
Description:
Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12193R-A750)
Fournisseur:
Bioss
Description:
Transcription factor required for formation of positional identity in the developing retina, regionalization of the optic chiasm and morphogenesis of the kidney. Can neuralize ectodermal cells directly By similarity. Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator. Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. Probable transcription factor involved in embryogenesis and somatogenesis. FOXD1 is involved in regulating inflammation as well as kidney and retinal development. FOXD1 regulates the activity of NFAT and NFkB. Deficiency of FOXD1 results in multiorgan systemic inflammation, exaggerated Th cell-derived cytokine production, and T cell proliferation in autogolgous MLRs. In kidneys, FOXD1 controls the production of signals required for the normal transition of induced mesenchyme into tubular epithelium and full growth and branching of the collecting system. Deletion of FOXD1 results in renal abnormalities. FOXD2 acts as a modulator of T cell activation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12193R-CY5)
Fournisseur:
Bioss
Description:
Transcription factor required for formation of positional identity in the developing retina, regionalization of the optic chiasm and morphogenesis of the kidney. Can neuralize ectodermal cells directly By similarity. Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator. Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. Probable transcription factor involved in embryogenesis and somatogenesis. FOXD1 is involved in regulating inflammation as well as kidney and retinal development. FOXD1 regulates the activity of NFAT and NFkB. Deficiency of FOXD1 results in multiorgan systemic inflammation, exaggerated Th cell-derived cytokine production, and T cell proliferation in autogolgous MLRs. In kidneys, FOXD1 controls the production of signals required for the normal transition of induced mesenchyme into tubular epithelium and full growth and branching of the collecting system. Deletion of FOXD1 results in renal abnormalities. FOXD2 acts as a modulator of T cell activation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1432R-FITC)
Fournisseur:
Bioss
Description:
Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1432R-A680)
Fournisseur:
Bioss
Description:
Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1432R-A750)
Fournisseur:
Bioss
Description:
Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute non-lymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.
Fournisseur:
Biotium
Description:
CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute non-lymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.
Fournisseur:
Biotium
Description:
CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute non-lymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.
Numéro de catalogue:
(ENZOADIKAMST001E)
Fournisseur:
ENZO LIFE SCIENCES
Description:
β-Catenin, a vertebrate homologue of Drosophila armadillo encoded by the CTNNB1 gene, performs two functions in the cell: mediating cell-cell adhesion by association between E-cadherin and the cytoskeleton, and acting as a downstream transcriptional activator of Wnt signaling, a key player in such functions as embryonic development, the induction of cell polarity, and the determination of cell fate. In the absence of Wnt signaling, glycogen synthase kinase-3β (GSK-3β) phosphorylates any free β-catenin at the amino terminus. This results in adenomatous polyposis coli tumor suppressor protein (APC)-mediated β-catenin degradation via the ubiquitin-proteosome pathway. Wnt signaling stabilizes β-catenin by inhibiting the activity of GSK-3β and preventing β-catenin degradation. β-catenin forms complexes with DNA-binding proteins such as T-cell factor (Tcf) and lymphocyte-enhancer factor (Lef), which promote expression of a variety of target genes, including c-myc and cyclin D1.
UOM:
1 * 1 EA
New Product
Numéro de catalogue:
(BOSSBS-1476R-A555)
Fournisseur:
Bioss
Description:
This multifunctional protein catalyses the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11062R-CY3)
Fournisseur:
Bioss
Description:
CYTIP is a cytoplasmic protein that is involved in lymphocytic cell adhesion. Expressed primarily in hematopoetic cells, CYTIP regulates the activity of cytohesin-1 (an integrin-activating protein involved in cell adhesion) by mediating its recruitment to the leukocyte membrane. Through its ability to bind cytohesin-1, CYTIP is able to sequester it to the cytoplasm, thereby preventing cytohesin-1 translocation to lymphocytes and interrupting the flow of information in the cell adhesion pathway. CYTIP can be recruited from the cytoplasm to the membrane by leukocyte integrins which interact with CYTIP through its PDZ domain. After membrane translocation, CYTIP can be re-located to the cytoplasm via exposure to a phorbol ester. Additionally, CYTIP associates with SNX27 (sorting nexin 27) and helps to coordinate trafficking and signaling complexes. Up-regulation of CYTIP is observed in maturing dendritic cells, suggesting a possible role in developmentally-controlled cell adhesion.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11062R-CY5)
Fournisseur:
Bioss
Description:
CYTIP is a cytoplasmic protein that is involved in lymphocytic cell adhesion. Expressed primarily in hematopoetic cells, CYTIP regulates the activity of cytohesin-1 (an integrin-activating protein involved in cell adhesion) by mediating its recruitment to the leukocyte membrane. Through its ability to bind cytohesin-1, CYTIP is able to sequester it to the cytoplasm, thereby preventing cytohesin-1 translocation to lymphocytes and interrupting the flow of information in the cell adhesion pathway. CYTIP can be recruited from the cytoplasm to the membrane by leukocyte integrins which interact with CYTIP through its PDZ domain. After membrane translocation, CYTIP can be re-located to the cytoplasm via exposure to a phorbol ester. Additionally, CYTIP associates with SNX27 (sorting nexin 27) and helps to coordinate trafficking and signaling complexes. Up-regulation of CYTIP is observed in maturing dendritic cells, suggesting a possible role in developmentally-controlled cell adhesion.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1476R-A750)
Fournisseur:
Bioss
Description:
This multifunctional protein catalyses the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).
UOM:
1 * 100 µl
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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