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Human casein

SKU : BHP10506049

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CUSABIO TECHONOLOGY LLC

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Mfr.No.	CSB-NP008801h
Description	Casein contains a fairly high number of proline residues, which do not interact. There are also no disulfide bridges. As a result, it has relatively little tertiary structure. It is relatively hydrophobic, making it poorly soluble in water. It is found in milk as a suspension of particles called "casein micelles" which show only limited resemblance with surfactant-type micellae in a sense that the hydrophilic parts reside at the surface and they are spherical. However, in sharp contrast to surfactant micelles, the interior of a casein micelle is highly hydrated. The caseins in the micelles are held together by calcium ions and hydrophobic interactions. Several models account for the special conformation of casein in the micelles (Dalgleish, 1998). One of them proposes the micellar nucleus is formed by several submicelles, the periphery consisting of microvellosities of κ-casein (Walstra, 1979; Lucey, 2002). Another model suggests the nucleus is formed by casein-interlinked fibrils (Holt, 1992). Finally, the most recent model (Horne, 1998) proposes a double link among the caseins for gelling to take place. All three models consider micelles as colloidal particles formed by casein aggregates wrapped up in soluble κ-casein molecules.
Alternative Names	N/A
Regulatory	RUO
Relevance	Casein contains a fairly high number of proline residues, which do not interact. There are also no disulfide bridges. As a result, it has relatively little tertiary structure. It is relatively hydrophobic, making it poorly soluble in water. It is found in milk as a suspension of particles called "casein micelles" which show only limited resemblance with surfactant-type micellae in a sense that the hydrophilic parts reside at the surface and they are spherical. However, in sharp contrast to surfactant micelles, the interior of a casein micelle is highly hydrated. The caseins in the micelles are held together by calcium ions and hydrophobic interactions. Several models account for the special conformation of casein in the micelles (Dalgleish, 1998). One of them proposes the micellar nucleus is formed by several submicelles, the periphery consisting of microvellosities of κ-casein (Walstra, 1979; Lucey, 2002). Another model suggests the nucleus is formed by casein-interlinked fibrils (Holt, 1992). Finally, the most recent model (Horne, 1998) proposes a double link among the caseins for gelling to take place. All three models consider micelles as colloidal particles formed by casein aggregates wrapped up in soluble κ-casein molecules.
Source	Purified from Human milk
Form	Liquid
Protein Name	Human Casein
Bioactivity	Not test
Biological Activity Comment	Not test
Nature	Native
Protein Length	Full length protein

Research Area	Cell Biology

Buffer	PBS, pH 7.4
Format	Liquid
Purity	>95% (SDS-PAGE)
Storage	Aliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles.
Storage Buffer	PBS, pH 7.4

Applications	SDS, ELISA, WB, SDS-PAGE

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SKU	Supplier No.	Size	Your price	Quantity
BHP10506049	CSB-NP008801h	10mg	$3605		Add to Cart
BHP10506049	CSB-NP008801h	1mg	$450		Add to Cart

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