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Image Unavailable-78307-1KG

Silica gel PS 2-6 mm torkmedel, med indikator, Fluka™

Artikel nummer : (78307-1KG)
Leverantör: Honeywell Chemicals
Beskrivning: Contains ≤0.25% CuCl₂ as additive
UOM: 1 * 1 kg
Product Image-BSENR-1697-100

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

Artikel nummer : (BSENR-1697-100)
Leverantör: Biosensis
Beskrivning: 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).
UOM: 1 * 100 µl
Image Unavailable-10657.22

Bismuth(III) nitrate, hydrate ≥99.999%, Puratronic®

Leverantör: Thermo Fisher Scientific
Beskrivning: It is used in electronic ceramics and fluorescent paints. It is employed as an oxidant for selective oxidation of sulfides to sulfoxides, as a nitrating reagent for synthesizing nitro aromatic compounds, and as a precursor for Dragendorff reagent for use in TLC stain and for testing the presence of alkaloids. On silica gel support, it has been reported to be an efficient catalyst for the Biginelli reaction.

Säkerhetsdatablad Certifikat

Product Image-ACRO360122500

Kiselgel C18-RP 17% C (∼0,7 mmol/g) Ø 48-65 µm

Leverantör: Thermo Fisher Scientific
Beskrivning: Kiselgel C18-RP 17% C (∼0,7 mmol/g) Ø 48-65 µm

Säkerhetsdatablad

Image Unavailable-7511-04

SPE-kolonner för speciella applikationer, J.T.Baker®, BAKERBOND spe™ PCB-A

Artikel nummer : (7511-04)
Leverantör: Avantor
Beskrivning: Denna Solid Phase Extraction Column är framtagen för extraktion av PCB:er i olja (smutsiga prover) i kombination med SPE kiselgel.
UOM: 1 * 50 Items

Certifikat


Product Image-13-2500-01

Peqlab peqGOLD, DNA Clean-up, Gel Extraction Kits

Artikel nummer : (13-2500-01)
Leverantör: VWR Chemicals
Beskrivning: Purifies DNA bands 70 bp to 20 kb in length from agarose gels. The DNA band of interest is excised from the gel, dissolved in binding buffer, and efficiently processed in a peqGOLD DNA column. >90% recovery. Elution volume: 30 to 50 µl.
UOM: 1 * 50 Tests

Säkerhetsdatablad Certifikat


Product Image-ACRO360112500

Kiselgel C18-RP 23% C (∼1 mmol/g) Ø 40-63 µm

Leverantör: Thermo Fisher Scientific
Beskrivning: CAS No.: 71889-02-6

Säkerhetsdatablad

Image Unavailable-BOSSBS-13736R-CY7

Anti-ADAM13 Rabbit Polyclonal Antibody (Cy7®)

Artikel nummer : (BOSSBS-13736R-CY7)
Leverantör: Bioss
Beskrivning: 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
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-A647

Anti-ADAM13 Rabbit Polyclonal Antibody (Alexa Fluor® 647)

Artikel nummer : (BOSSBS-13736R-A647)
Leverantör: Bioss
Beskrivning: 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
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-FITC

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

Artikel nummer : (BOSSBS-13736R-FITC)
Leverantör: Bioss
Beskrivning: 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
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-A488

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

Artikel nummer : (BOSSBS-13736R-A488)
Leverantör: Bioss
Beskrivning: 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
UOM: 1 * 100 µl
Product Image-BOHLV1994-08

Desiccator cabinet, SICCO wall

Artikel nummer : (BOHLV1994-08)
Leverantör: Bohlender
Beskrivning: Transparent PPMA cabinet with reinforced aluminium frame, unit has a door with a foam rubber gasket and magnetic strip. Designed for storing or drying humidity sensitive products using silica gel. The controlled environment inside the desiccator is ideal for storing reference materials, retained samples, metallographic specimens, tobacco and DNA-samples.
UOM: 1 * 1 Items
Image Unavailable-BOSSBS-13736R-A555

Anti-ADAM13 Rabbit Polyclonal Antibody (Alexa Fluor® 555)

Artikel nummer : (BOSSBS-13736R-A555)
Leverantör: Bioss
Beskrivning: 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
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-CY5

Anti-ADAM13 Rabbit Polyclonal Antibody (Cy5®)

Artikel nummer : (BOSSBS-13736R-CY5)
Leverantör: Bioss
Beskrivning: 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
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-13736R-HRP

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

Artikel nummer : (BOSSBS-13736R-HRP)
Leverantör: Bioss
Beskrivning: 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
UOM: 1 * 100 µl
Product Image-MILFLSKMTAE50

Montage® Gel Extraction Kit

Leverantör: Merck
Beskrivning: The device utilises gel compression to extract DNA from the agarose. Centrifugal force collapses the gel structure, drives the agarose through a small orifice in the gel nebulizer and the resultant gel slurry is sprayed into the sample filter cup.

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Lager för denna produkt är begränsat, men kan vara tillgänglig i ett lager nära dig. Se till att du är inloggad på hemsidan så att tillgängligt lager kan visas. Om call fortfarande visas och du behöver hjälp, ring oss på 08-621 34 20.
VWR International AB säljer bara etanol till skattebefriade kunder. Denna produkt ä reglerad enligt svensk lagstiftning. Om ytterligare information krävs av dig kommer du att kontaktas via e-post.
VWR International AB säljer bara etanol till skattebefriade kunder.
Denna produkt ä reglerad enligt svensk lagstiftning. Om ytterligare information krävs av dig kommer du att kontaktas via email.
Produkten har blockerats av din organisation. Vänligen kontakta din inköpsavdelning för mer information.
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Denna produkt är inte längre tillgänglig. Alternativ kan vara tillgängliga genom att söka med VWR art.nr ovan. Om du behöver ytterligare hjälp, ring VWR Kundservice på 08-621 34 20.
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