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Product Image-ACRO360180100

Silica gel, functionalized, Amino-3 ∼1,4 mmol/g, Ø 40-63 micron

Dodavatel: Thermo Scientific
Popis: CAS No.: 71888-97-6

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Image Unavailable-79297-100G

Amino-functionalized silica gel, spherical 40-75 μm particle size, Supelco®

Dodavatel: Merck
Popis: Amino-functionalized silica gel, spherical 40-75 μm particle size, Supelco®

Nové řešení transparentnosti pro evropské zákazníky

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Image Unavailable-SIAL630063-25G

Silica gel, functionalized, Aluminum chloride 1,5 mmol/g 40-63 μm, Sigma-Aldrich®

Dodavatel: Merck
Popis: Application: Silica-bound Lewis acid. Catalyst for Friedel-Crafts reactions.

Product Image-552-0254

HPTLC Plates, Nano Silica Gel 60, Modified Layers, Nano-SIL NH₂

Dodavatel: MACHEREY-NAGEL
Popis: Amino-modified HPTLC silica layers are available as glass plates or ALUGRAM® aluminium sheets. They are ideal for the separation of vitamins, sugars, steroids, purine derivatives, xanthines, phenols, nucleotides, and pesticides.

Product Image-552-0235

HPTLC plates, nano silica gel 60, modified layers, Nano-SIL C18

Dodavatel: MACHEREY-NAGEL
Popis: Octadecyl-modified HPTLC silica glass plates are recommended for alkaloids, amino acids, preservatives, optical brighteners, barbiturates, polycyclic aromatic hydrocarbons (PAH), drugs, peptides, flavonoids, phenols, indole derivatives and steroids.

Product Image-1.13725.0001

HPTLC plates silica gel 60, RP-modified layers, glass backed

Dodavatel: Merck
Popis: Our NH₂, CN- and DIOL-modified silica sorbents are less polar then conventional silica phases, making them ideal for separating hydrophilic or charged substances. Our moderately polar cyano- and diol-modified silica plates can be used for both normal phase and reversed phase systems. An alternative to PEI cellulose, amino-modified NH₂ plates provide weak basic ion exchange characteristics with special selectivity for charged compounds.

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Image Unavailable-554-0918

TSKgel® reversed phase columns

Dodavatel: TOSOH Bioscience
Popis: These silica- and polymer-based columns are ideal for reversed-phase applications such as pharmaceutical drugs, forensic compounds, derivatised amino acids, carbohydrates, steroids, lipids and fatty acids. Depending on their molecular weight, peptides may be analysed with the 80 to 140 Å silica-based columns, while proteins require a larger pore size column (200 to 300 Å).

Product Image-1.13192.0001

HPTLC plates silica gel 60, modified CN, DIOL, NH₂, glass backed

Dodavatel: Merck
Popis: CN- and DIOL-modified silica plates are moderately polar that are suitable for both normal and reversed phase systems. The amino modified NH₂ plate provides weak basic ion exchange characteristics with special selectivity for charged compounds offering an alternative to PEI cellulose.

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Product Image-BSENC-1698-100

Anti-Lamin A/C Chicken Polyclonal Antibody

Katalogové číslo: (BSENC-1698-100)
Dodavatel: Biosensis
Popis: The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).
Měrná jednotka: 1 * 100 µl
Product Image-552-0240

TLC plates, special layers, glass backing, CHIRALPLATE

Dodavatel: MACHEREY-NAGEL
Popis: These glass plates with a special layer are used for TLC enantiomer separations (e.g. amino acids, thiazolidine derivatives, dipeptides, lactones, α-hydroxycarboxylic acids).

Certifikáty

Product Image-BSENR-1697-100

Anti-Lamin A/C, whole molecule Rabbit Polyclonal Antibody

Katalogové číslo: (BSENR-1697-100)
Dodavatel: Biosensis
Popis: The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).
Měrná jednotka: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-CY5

Anti-ADAM13 Rabbit Polyclonal Antibody (Cy5®)

Katalogové číslo: (BOSSBS-13736R-CY5)
Dodavatel: Bioss
Popis: ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
Měrná jednotka: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-HRP

Anti-ADAM13 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Katalogové číslo: (BOSSBS-13736R-HRP)
Dodavatel: Bioss
Popis: ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
Měrná jednotka: 1 * 100 µl
Product Image-15173LX

Silikagel, DAVISIL® 923 suitable for use in the testing of petroleum products by IP and ASTM methods

Katalogové číslo: (15173LX)
Dodavatel: VWR Chemicals
Popis: DAVISIL® 923 Chromatographic Silica is a synthetic, amorphous silica in granular form.
Měrná jednotka: 1 * 1 kg

Bezpečnostní list Certifikáty


Image Unavailable-BOSSBS-13736R-A488

Anti-ADAM13 Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Katalogové číslo: (BOSSBS-13736R-A488)
Dodavatel: Bioss
Popis: ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
Měrná jednotka: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-FITC

Anti-ADAM13 Rabbit Polyclonal Antibody (FITC (Fluorescein Isothiocyanate))

Katalogové číslo: (BOSSBS-13736R-FITC)
Dodavatel: Bioss
Popis: ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
Měrná jednotka: 1 * 100 µl
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Omezené množství produktu na skladě. Zboží může být k dispozici v jiném skladě poblíž vašeho sídla. Přesvědčte se, že jste přihlášení na stránky, abyste mohli vidět dostupné položky na skladě. Pokud je stále zobrazeno call a potřebujete asistenci, volejte na číslo 321 570 321.
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