ProteinChip® Biology System

ProteinChip® Biology System
 4.0/5.0 (1 review)

Ciphergen BioSystems S.A

On-chip protein isolation and identification Ciphergen’s ProteinChip® Biology System is a complete solution for basic proteomics research. Consisting of instrumentation, ProteinChip Arrays an...read more

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Ciphergen BioSystems S.A

Reviews

Sankar Baruah


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Member since 2004

Organization:
University of Iowa, Ophthalmology
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RATING: 4.0

  • 4 out of 5EASE OF USE
  • 4 out of 5AFTER SALES SERVICE
  • 4 out of 5VALUE FOR MONEY




Review date: 13 May 2004

ProteinChip® Biology System

"Good product for Biologists and other non - Mass Spectrometists to get mass information on biopolymers"

Description

 

On-chip protein isolation and identification

Ciphergen’s ProteinChip® Biology System is a complete solution for basic proteomics research. Consisting of instrumentation, ProteinChip Arrays and software, the ProteinChip Biology System gives you the ability to quickly compare the presence and abundance of individual proteins in crude samples, characterize, isolate and identify individual proteins, investigate antibody-antigen recognition, and study receptor-ligand interactions and DNA-protein associations.

Using SELDI technology, the ProteinChip Biology System brings new analytical capabilities into your lab, such as:

  • Quickly resolve mixtures of proteins and protein fragments that are either too small or have extreme pI’s for gel electrophoresis
  • Develop fast purification methods without columns using a variety of surface chemistries and buffer conditions

The ProteinChip Biology System enables you to quickly determine proteomic changes in response to specific stimuli, and is unique in its ability to analyze trace (low femtomole) analytes from crude, low-volume samples.

Of proven use as a stand-alone device in hundreds of laboratories worldwide, Ciphergen’s ProteinChip Biology System is also an excellent complement to SELDI-adapted tandem mass spectrometry installations, enabling top-down protein identification based on primary sequence data and high-resolution mapping of protein-protein interactions

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