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52468

Sigma-Aldrich

C-Phycocyanin

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About This Item

UNSPSC Code:
12352108
NACRES:
NA.32

concentration

≥10.0 mg/mL (UV)

Quality Level

100

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 Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

ISHL Indicated Name

Substances Subject to be Indicated Names

ISHL Notified Names

Substances Subject to be Notified Names

JAN Code

52468-1MG-F:
52468-5MG-F:
52468-BULK-F:
52468-VAR-F:

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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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
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
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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