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Sigma-Aldrich

C-Phycocyanin

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About This Item

UNSPSC Code:
12352108
NACRES:
NA.32

concentration

≥10.0 mg/mL (UV)

technique(s)

electrophoresis: suitable

fluorescence

λex 609 nm; λem 643 nm in 0.1 M phosphate pH 7.2

suitability

in accordance for gel electrophoresis

storage temp.

2-8°C

General description

The product is suspended in 150 mM sodium phosphate, 60% ammonium sulfate, 1 mM EDTA, 1 mM sodium azide, pH 7.0 and must be dialyzed against conjugation buffer or PBS before conjugation.

Application

C-Phycocyanin (CPC), a pigment-protein complex from the light-harvesting phycobiliprotein family, may be used in immunoassay kit development and to study its properties as a light harvesting protein.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Analysis Note

A620/A280 >3.5, A651/A620 <0.3

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Faceshields, Gloves, Goggles


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Jordan M Womick et al.
The journal of physical chemistry. B, 113(48), 15771-15782 (2009-11-12)
The electronic structure and photoinduced relaxation dynamics of the cyanobacterial light harvesting protein, C-Phycocyanin (CPC), are examined using transient grating and two-dimensional (2D) photon echo spectroscopies possessing sub-20 fs time resolution. In combination with linear absorption and fluorescence measurements, these
H Scheer et al.
Molecular microbiology, 68(2), 263-276 (2008-02-21)
Biliproteins are a widespread group of brilliantly coloured photoreceptors characterized by linear tetrapyrrolic chromophores, bilins, which are covalently bound to the apoproteins via relatively stable thioether bonds. Covalent binding stabilizes the chromoproteins and is mandatory for phycobilisome assembly; and, it
Michaela Kupka et al.
Biochimica et biophysica acta, 1777(1), 94-103 (2007-11-27)
Optical spectroscopic properties of the covalently linked chromophores of biliproteins are profoundly influenced by the state of the protein. This has been used to monitor the urea-induced denaturation of C-phycocyanin (CPC) from Mastigocladus laminosus and its subunits. Under equilibrium conditions
Lijin Tian et al.
The journal of physical chemistry. B, 117(38), 11000-11006 (2012-12-18)
Cyanobacteria are oxygen-evolving photosynthetic organisms that harvest sunlight and convert excitation energy into chemical energy. Most of the light is absorbed by large light harvesting complexes called phycobilisomes (PBs). In high-light conditions, cyanobacteria switch on a photoprotective mechanism called non-photochemical
Rasiah Pratheepa Kumari et al.
Biological trace element research, 151(1), 59-67 (2012-10-23)
The present investigation is aimed to evaluate the anticataractogenic potential of C-phycocyanin (C-PC), extracted and purified from Spirulina platensis. Enucleated rat lenses were maintained in vitro in Dulbecco's modified Eagle medium (DMEM). Group I contained DMEM, Group II and Group

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