A2764
Albumin from porcine serum
lyophilized powder, 96-99% (agarose gel electrophoresis)
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About This Item
Prodotti consigliati
Origine biologica
Porcine
Livello qualitativo
Saggio
96-99% (agarose gel electrophoresis)
Stato
lyophilized powder
tecniche
ELISA: suitable
N° accesso UniProt
Temperatura di conservazione
2-8°C
Informazioni sul gene
Porcine ... ALB(396960)
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Descrizione generale
Albumin, the most abundant plasma protein (60%), is synthesized in the liver. It performs several functions. Porcine serum albumin (PSA), a globular protein, is a major allergen in pork.
Applicazioni
Albumin from porcine serum:
- may be used in metal competition studies to get loaded with copper(II)/Cu(II) for affinity constant measurements and to investigate its secondary specific Cu(II) binding site
- has been used as a macromolecule marker for colostrum feeding and as a purified antigen to measure porcine serum albumin (PSA) in milk and plasma by quantitative immunoelectrophoresis
- has been used in the production of anti-albumin antisera for the detection of meats of different animal species in commercial hamburger samples using dot-ELISA (enzyme-linked immunosorbent assay)
Prodotto comparabile
N° Catalogo
Descrizione
Determinazione del prezzo
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
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A Macedo-Silva et al.
Meat science, 56(2), 189-192 (2000-10-01)
The use of low cost meats to adulterate meats and meat products has been reported. Appropriate methods of analysis then are needed in order to detect this practice. The dot-ELISA method was used to identify the meat of different animal
W Bal et al.
Journal of inorganic biochemistry, 70(1), 33-39 (1998-07-14)
Circular dichroism and electron spin resonance spectroscopy are used to investigate the second specific metal binding site on human, bovine and porcine albumins. Ni(II), Zn(II) and Cd(II) can displace Cu(II) from the second Cu(II) site but not from the first
Robert Kumagai et al.
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