Waters Technologies Corporation

Xiaoxiao Liu

Matthew A Lauber

Anna Boardman

Mathew H DeLano

Beatrice W Muriithi

Jonathan L Belanger

Moon Chul Jung

Edouard S P Bouvier

Michael Donegan

Robert Birdsall

Erin E Chambers

Christopher John Hughes

Michael Lavallee

Wenhao Zhu

Yun Wang Alelyunas

Mary Elizabeth Lame

David Dao

Paula Orens

Micah Watt

Caitlin Dunning

A device for processing samples is disclosed. Interior surfaces of the device, which come in contact with fluids, define wetted surfaces. A portion of the wetted surfaces are coated with an alkylsilyl coating having the Formula I: R, R, R, R, R, and Rare each independently selected from (C-C)alkoxy, —NH(C-C)alkyl, —N((C-C)alkyl), OH, OR, and halo. Rrepresents a point of attachment to the interior surfaces of the fluidic system. At least one of R, R, R, R, R, and Ris OR. X is (C-C)alkyl, —O[(CH)O]—, —(C-C)[NH(CO)NH(C-C)]—, or —(C-C)[alkylphenyl(C-C)alkyl]-.

Use of vapor deposition coated flow paths for improved analytical analysis

The present technology relates to a customizable sample preparation device (e.g., liquid sample preparation device, such as a purification, clean-up, or separation device). In particular, the present technology relates to customizable devices formed from modular segments tailored to address one or more of the following: to optimize different sample and elution volumes, to incorporate various connection mechanisms to liquid handlers, to incorporate various liquid dispensing flow conditions, and to fulfill broad applications through the selection of specific resin for sample preparation. Some embodiments are directed to affinity capture devices, such as for example, Protein A affinity capture devices, utilizing a polymethacrylate-based resin. Other resins as well as other materials for processing a liquid sample are described herein.

Modular sample preparation devices and methods

A sample preparation device is provided for enriching a component of a sample. The sample preparation device includes a surface in fluid communication with the sample, an alkylsilyl coating disposed on the surface, and an affinity ligand or an enzyme covalently bonded to the alkylsilyl coating.

Coatings with immobilized affinity ligands and enzymes and use thereof in liquid chromatography assays

The present technology relates to a method for improved recovery of phosphorylated compounds (e.g., phosphorylated glycans). In particular, the present technology utilizes certain chelator additives in a solution to wash and elute the phosphorylated compounds from a solid phase extraction cartridge.

Chelator based eluents for solid phase extraction of phosphorylated compounds

The present disclosure relates to a method of analyzing a sample comprising a hydrophobic molecule. The method includes preparing an aqueous solution comprising the sample. The method also includes placing the solution in contact with a polypropylene substrate having a deactivated surface that reduces adsorption of the hydrophobic molecule relative to a polypropylene substrate that has not been deactivated. The method also includes analyzing the sample.

Methods of use for low-bind polypropylene plates and vials

A device for processing samples is disclosed. Interior surfaces of the device, which come in contact with fluids, define wetted surfaces. A portion of the wetted surfaces are coated with an alkylsilyl coating having the Formula I: R, R, R, R, R, and Rare each independently selected from (C-C)alkoxy, &#x2014;NH(C-C)alkyl, &#x2014;N((C-C)alkyl), OH, OR, and halo. Rrepresents a point of attachment to the interior surfaces of the fluidic system. At least one of R, R, R, R, R, and Ris OR. X is (C-C)alkyl, &#x2014;O[(CH)O]&#x2014;, &#x2014;(C-C)[NH(CO)NH(C-C)]&#x2014;, or &#x2014;(C-C)[alkylphenyl(C-C)alkyl]&#x2014;.

A method of capturing human immunoglobulin Fc domains in a biofluid sample is provided. The method includes providing an affinity capture device. The affinity capture device includes a surface having an aptamer that is at least 80% identical to SEQ ID NO 1 immobilized onto the surface of the affinity capture device. The biofluid sample is diluted with a binding buffer. The binding buffer includes (A) tris(hydroxymethyl)aminomethane (Tris), trimethylamine (TES), 2-ethanesulfonic acid (MES), or 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES); (B) a magnesium cation at a concentration between about 10 &#x3bc;M to about 20 mM; and (C) a total monovalent cation concentration from 0 to no greater than 100 mM. The human immunoglobulin Fc domains in the biofluid sample are adsorbed to the aptamer with the binding buffer.

Aptamer based affinity capture methods for the selective enrichment of human immunoglobulin Fc domains

The present disclosure relates to protein arrays and methods of using the same for the detection, quantification and characterization of biomolecules that specifically bind to the array among various other biomolecules in a biological sample. Specifically, the present disclosure relates to protein arrays that include a plurality of immunoglobulin molecules derived from shark single-domain heavy chain antibody lacking light-chains but including at least one variable antigen-binding domain with a binding site for an antigen. The immunoglobulin molecules are immobilized on a substrate via a linker. Further encompassed herein are diagnostic devices and kits, comprising the protein array and methods of using same.

Growing community of inventors

Natick, MA, United States of America

Xiaoxiao Liu