C0880
Conalbumin from chicken egg white
Iron complex
Synonym(s):
Ovotransferrin
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About This Item
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biological source
chicken egg white
Quality Level
Assay
≥95% (agarose gel electrophoresis)
form
powder
technique(s)
gel permeation chromatography (GPC): suitable
UniProt accession no.
storage temp.
−20°C
Gene Information
chicken ... TF(396241)
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General description
Iron-carrying proteins conalbumin and serum transferrin are synthesized with identical 19-amino-acid leader sequences that are removed during protein maturation. The leader sequences are presumably involved in secretion of the proteins by endoplasmic reticulum.
Application
Conalbumin (CA) is a monomeric glycoprotein that makes up approximately 13% of the albumin found in egg white. The iron complex of CA is more stable to chemical and physical treatments when compared to the uncomplexed proteins. At near neutral conditions, urea denaturation of CA modifies but does not destroy the iron complex.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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The denaturation of proteins. IV. Conalbumin and iron(III)-conalbumin in urea solution.
Biochimica et biophysica acta, 71, 109-123 (1963-04-02)
The resistances of conalbumin and its iron complex to physical and chemical treatments.
Archives of biochemistry and biophysics, 92, 44-52 (1961-01-01)
The Journal of biological chemistry, 253(11), 3771-3774 (1978-06-10)
The NH2-terminal sequences of egg white conalbumin and chicken serum transferrin were examined and found to be identical. Conalbumin, when synthesized in a rabbit reticulocyte cell-free translation system, was found to contain an NH2-terminal extension of 19 amino acid residues.
Biochimica et biophysica acta, 1820(3), 244-255 (2011-06-23)
In vertebrates, serum transferrins are essential iron transporters that have bind and release Fe(III) in response to receptor binding and changes in pH. Some family members such as lactoferrin and melanotransferrin can also bind iron while others have lost this
Biochimica et biophysica acta, 1820(3), 203-211 (2011-08-23)
Transferrins are a group of iron-binding proteins including serum transferrin, lactoferrin and ovotransferrin. The structures of transferrins are discussed. The typical transferrin molecules are folded into two homologous lobes. X-ray crystallography revealed that each lobe is further divided into two
Chromatograms
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