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Merck
CN

MSHVN4B

Multiscreen® 96 well Plate, hydrophilic PVDF membrane

pore size 0.45 μm

别名:

Hydrophilic 96-Well Plate, PVDF 96-Well Plate

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关于此项目

UNSPSC Code:
41104923
NACRES:
NB.22
eCl@ss:
32039006
Material:
Durapore PVDF membrane, flat bottom wells, white Barex® plate (co-polymer)
Pore size:
0.45 μm pore size
Binding type:
low binding surface

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Quality Level

400

material

Durapore PVDF membrane, flat bottom wells, white Barex® plate (co-polymer)

description

Receptor binding assays on whole cells and cell fragments, protein kinase/phosphatase precipitation assays, bead/resin based assays

usage

Automated

feature

hydrophilic, lid

packaging

pkg of 10 plates, pkg of 50 plates

manufacturer/tradename

MultiScreen®

technique(s)

activity assay: suitable (protein kinase/phosphatase precipitation), bead-based assay: suitable, ligand binding assay: suitable, low protein binding filtration: suitable, receptor binding assay: suitable

H

14.4 mm

L

128 mm

W

85.5 mm

filtration area

0.28 cm2

plate size

96 wells

well maximum volume

300 μL

working volume

50-250 μL

matrix

Durapore®

pore size

0.45 μm pore size

application(s)

sample preparation

binding type

low binding surface

compatibility

centrifuge & manifold

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相关类别

Application

MultiScreen® HTS HV Filter Plate, 0.45 μm, opaque, non-sterile has been used in the maltose-binding protein (MBP)-E6 and E6 association protein (AP) binding assay.

Features and Benefits

MultiScreen® Plates feature:
  • High throughput screening
  • The American National Standards Institute (ANSI) and the Society of Biomolecular Screening (SBS) standards compliance
  • Rigid sidewalls
  • Barcode-labeling capability
  • Design that prevents cross-well contamination

Legal Information

Barex is a registered trademark of INEOS Barex AG
Durapore is a registered trademark of Merck KGaA, Darmstadt, Germany
MULTISCREEN is a registered trademark of Merck KGaA, Darmstadt, Germany

存储类别

10-13 - German Storage Class 10 to 13

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Anne Rietz et al.
PloS one, 11(2), e0149845-e0149845 (2016-02-26)
The human papillomavirus (HPV) HPV E6 protein has emerged as a central oncoprotein in HPV-associated cancers in which sustained expression is required for tumor progression. A majority of the E6 protein interactions within the human proteome use an alpha-helix groove

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