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Référence Produit: (BOSSBS-6815R-A350)
Fournisseur: Bioss
Description: LRRC15 may contribute to regulation of cell-matrix adhesion interactions with respect to astrocyte recruitment around senile plaques in Alzheimer's disease brain. LRRC15 is induced by EWS-WT1(+KTS) in the tumor DSRCT and may play a role in cellular invasion.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-6815R-FITC)
Fournisseur: Bioss
Description: LRRC15 may contribute to regulation of cell-matrix adhesion interactions with respect to astrocyte recruitment around senile plaques in Alzheimer's disease brain. LRRC15 is induced by EWS-WT1(+KTS) in the tumor DSRCT and may play a role in cellular invasion.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-3619R-A350)
Fournisseur: Bioss
Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-3619R-A488)
Fournisseur: Bioss
Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-0107R-CY5.5)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-10429R-CY5)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-10429R-A555)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-0076R-CY7)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-0076R-A350)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-3619R-CY5)
Fournisseur: Bioss
Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-10429R-CY7)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-0107R-CY7)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-10429R)
Fournisseur: Bioss
Description: The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
UOM: 1 * 100 µl


Référence Produit: (734-0116)
Fournisseur: Corning
Description: Corning® BioCoat®, Plaque de culture cellulaire, Plaques à 96 puits
UOM: 1 * 5 Pce

Certificats. Environmentally Preferable


Référence Produit: (ENZOADI905803100)
Fournisseur: ENZO LIFE SCIENCES
Description: The beta-amyloid peptide (beta A4), proteolytically released from the amyloid precursor protein (APP), provides the principal component of senile plaques in Alzheimer's disease. Cleavage of APP by alpha-secretase or alternatively by beta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, respectively, and the retention of corresponding membrane-anchored C-terminal fragments, C83 and C99. Subsequent processing of C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is nonamyloidogenic. Alternatively, presenilin/ nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59).
UOM: 1 * 100 µG


Référence Produit: (BOSSBS-6815R-CY3)
Fournisseur: Bioss
Description: LRRC15 may contribute to regulation of cell-matrix adhesion interactions with respect to astrocyte recruitment around senile plaques in Alzheimer's disease brain. LRRC15 is induced by EWS-WT1(+KTS) in the tumor DSRCT and may play a role in cellular invasion.
UOM: 1 * 100 µl


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