3225 Results for: "Rotating"

Supplier: Beckman Coulter

The Avanti™ J-15 series of benchtop centrifuges (refrigerated or ventilated) leverage the ultra harmonic technology, designed to protect your sample and increase workflow time efficiencies.

Supplier: MP Biomedicals

Storage: Store at -20 °C. Store Desiccated. Store Under Nitrogen. Protect from light.
5-Bromo-4-chloro-3-indolyl β-D-galactopyranoside, commonly known as X−Gal, is a histochemical substrate for β−galactosidase.
5-Bromo-4-Chloro-3-Indolyl-β-D-Galactopyranoside is used as indigogenic substrate for β-galactosidase, for detection of β-galactosidase-positive clones, and the identification of lac and bacterial colonies or phage plaques. It is the substrate of choice for blue-white selection of recombinant bacterial colonies with the lac+ genotype. X−Gal is cleaved by β−galactosidase to yield an insoluble blue precipitate. X−Gal is particularly useful in molecular biology applications to detect the activity of β−galactosidase which is frequently used as a reporter gene. In cloning, X−Gal is used to detect insertion of foreign DNA into the lacZ region of plasmid DNA using α-complementation which is based on vectors such as the pUC and the M13mp series that carry a fragment of the β-galactosidase gene encoding an α-fragment of β-galactosidase.

Supplier: Beckman Coulter

The Avanti™ J-15 series offers three rotors, the JS-4.750, JS-4.750µ and the JA-10.100.

Supplier: Upchurch Scientific

Wrenches are available in three standard sizes, to accommodate the hex headed fittings used throughout the analytical industry

Supplier: Beckman Coulter

The Avanti™ J-15 series of benchtop centrifuges (refrigerated or ventilated) leverage the ultra harmonic technology, designed to protect your sample and increase workflow time efficiencies.

Supplier: Heidolph NA, LLC

The Carousel 6 Plus™ Reaction Station simultaneously heats, stirs, and refluxes multiple samples under an inert atmosphere

Supplier: Thermo Scientific Chemicals

25G

Supplier: Thermo Scientific Chemicals

98%. 100g.

Supplier: MP Biomedicals

The FastDNA™ Spin Kit for Plant and Animals Tissues quickly and efficiently isolates high quality genomic DNA from plant and animal tissues.

Supplier: MP Biomedicals

The Fast DNA® SPIN Kit is used with the FastPrep®-24 or FastPrep® FP120 instrument to lyse and subsequently isolate DNA from up to 200 mg of almost any sample in less than 30 minutes.

Supplier: MP Biomedicals

Isolation of genomic DNA from plants, animals, bacteria, yeast, algae, and fungi.

Supplier: Thermo Scientific Chemicals

50G

Supplier: Thermo Scientific Chemicals

Powder

Supplier: Biosensis

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.

Supplier: Biosensis

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. Detects human, rat, other species not yet tested. By Dot Blot, MOAB-2 detected rat Aβ40 and human Aβ40, albeit with less affinity than for Aβ42 (Youmans KL et al., 2012).