Recherche de texte >
cell+culture+flasks
Imprimer
Votre recherche pour:
117 299 les résultats ont été trouvés
cell+culture+flasks
Numéro de catalogue:
(734-2386)
Fournisseur:
Corning
Description:
Hepatocyte culture medium is a serum-free, fully-defined medium optimised for hepatocyte differentiation.
UOM:
1 * 500 mL
Numéro de catalogue:
(BOSSBS-1135R-A680)
Fournisseur:
Bioss
Description:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labelling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr --> Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
UOM:
1 * 100 µl
Numéro de catalogue:
(STMC10985)
Fournisseur:
STEMCELL Technologies
Description:
For differentiation of human monocytes into dendritic cells.
UOM:
1 * 1 KIT
 Il s'agit d'un élément MarketSource. Des frais supplémentaires peuvent s'appliquer.
Fournisseur:
Corning
Description:
A complete range of classical cell culture media are available.
Fournisseur:
Thermo Fisher Scientific
Description:
Experience optimal performance with Thermo Scientific Nunc™ EasYDish™ dishes with Nunclon™ Supra surface treatment for culturing a wide variety of fastidious adherent cells.
Numéro de catalogue:
(BOSSBS-1967R-A488)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Fournisseur:
Biosensis
Description:
The Biosensis Mouse and Rat proNGF Rapid enzyme-linked immunosorbent assay (ELISA) Kit is a sandwich ELISA that allows the quantification of rodent full-length proNGF protein in less than 4 hours in cell culture supernatants, cell lysates and tissue homogenates only if used as directed. This ELISA Kit has also successfully been used on mouse urine samples (Ryu JC et al., 2018). Please refer to the kit protocol for specific use instructions for each substrate application.
This ELISA kit contains a recombinant mouse proNGF standard expressed in E.coli and consists of a pre-coated anti-proNGF capture antibody, a biotinylated anti-proNGF detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the concentration of proNGF present in samples and protein standards. A proNGF positive control (QC sample) is provided to assure consistent assay performance. This ELISA kit detects rat proNGF due to high degree of homology (96%) with mouse proNGF based on amino acid sequence, and the ability of this kit in detecting proNGF in rat PC12 cell lysates and rat brain tissue homogenate. In the absence of a true rat proNGF standard, results may be expressed as 'mouse proNGF equivalents'. This ELISA kit shows only 20% reactivity with the human form of proNGF and is therefore not suitable to quantify human proNGF. No cross-reactivity was observed with mature mouse NGF and full-length proBDNF when tested in assay buffer. The antibodies used in this ELISA kit bind epitopes within the pro-domain (capture) and mature domain (detection) of the protein, thus this ELISA assay does not detect the pro-domain peptide. This kit has not been tested for other applications. Sufficient amount of proNGF standard is supplied to allow for spike- and recovery experiments in order to validate this ELISA assay for other sample matrices if required.
Numéro de catalogue:
(BOSSBS-1967R-CY5)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(734-2385)
Fournisseur:
Corning
Description:
Endothelial culture medium is optimised to promote rapid growth (3- to 5-fold increase in cell number over five days) of endothelial cells from a variety of sources.
UOM:
1 * 1 KIT
Numéro de catalogue:
(BOSSBS-1967R-CY5.5)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1967R-A750)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localisation. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1967R-A350)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1967R-FITC)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BSENM-1586-100)
Fournisseur:
Biosensis
Description:
The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (Aβ) associated with the pathology characteristic of Alzheimer’s disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal Aβ accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for Aβ have been shown to actually detect intraneuronal APP and not Aβ exclusively. MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to Aβ residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide. MOAB-2 did not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice). Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for Aβ40 and Aβ42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10. In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal Aβ, distinct from Aβ associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.
UOM:
1 * 1 EA
Appel de prix
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'
 est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'
est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Ces articles ne peuvent être ajoutés au Panier. Veuillez contacter votre service client ou envoyer un e-mail à vwr.be@vwr.com
Une documentation supplémentaire peut être nécessaire pour l'achat de cet article. Un représentant de VWR vous contactera si nécessaire.
Ce produit a été bloqué par votre organisation. Contacter votre service d'achat pour plus d'informations.
Le produit original n'est plus disponible. Le remplacement représenté est disponible
Les produits marqués de ce symbole ne seront bientôt plus disponibles - vente jusqu'à épuisement de stock. Des alternatives peuvent être disponibles en recherchant le code article VWR indiqué ci-dessus. Si vous avez besoin d'une assistance supplémentaire, veuillez contacter notre Service Clientèle au 016 385 011.
|
|||||||||
Vue liste
