126621
Bovine Serum Albumin
Cohn Fraction, 30% Aqueous Solution
Sinónimos:
Albumin, Bovine Serum, Cohn Fraction, 30% Aqueous Solution
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About This Item
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Nombre del producto
Albumin, Bovine Serum, Cohn Fraction, 30% Aqueous Solution,
descripción
Merck USA index - 14, 8468
Ensayo
≥95% (agarose gel electrophoresis)
Formulario
liquid
fabricante / nombre comercial
Calbiochem®
condiciones de almacenamiento
OK to freeze
técnicas
MALDI-TOF: suitable
Condiciones de envío
ambient
temp. de almacenamiento
2-8°C
Categorías relacionadas
Descripción general
Albumin, Bovine Serum, (BSA) Cohn Fraction is purified by cold ethanol precipitation (Cohn extraction) and by heat treatment to remove lipids and fatty acids. It is a single carbohydrate-free polypeptide and the most abundant (comprising ~60%) of the plasma proteins. BSA regulates the maintenance of osmotic pressure.
BSA belongs to the serum albumin family, comprising three domains with two sub-domains under each. BSA is an α-helical, globular, and non-glycosylated protein with 17-disulfide bonds.
Acciones bioquímicas o fisiológicas
Bovine serum albumin (BSA) transports sparingly soluble physiological substances, especially long-chain fatty acids, bilirubin, drugs, hormones, and fatty acids. It acts as a blocking agent in enzyme-linked immunosorbent assay (ELISA). BSA is a vital component of the cell culture media and boosts embryonic stem cells (hESC) differentiation.
Advertencia
Toxicity: Standard Handling (A)
Forma física
30% solution in 0.8% NaCl, 0.1% NaN₃, pH 7.2, sterile-filtered.
Información legal
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 3
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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S Chodankar et al.
Physical review. E, Statistical, nonlinear, and soft matter physics, 77(3 Pt 1), 031901-031901 (2008-06-04)
Small-angle neutron scattering (SANS) and dynamic light scattering (DLS) have been used to study conformational changes in protein bovine serum albumin (BSA) due to perturbation in its native structure as induced by varying temperature and pressure, and in presence of
Yuhong Xiao et al.
Journal of immunological methods, 384(1-2), 148-151 (2012-06-27)
The enzyme-linked immunosorbent assay (ELISA) is an extremely common and powerful laboratory technique for detecting proteins by antibodies. Researchers frequently use bovine serum albumin (BSA) as a blocking agent to prevent non-specific binding of antigens and antibodies to the microtiter
Geoffrey L Francis
Cytotechnology, 62(1), 1-16 (2010-04-08)
Albumin has a long historical involvement in design of media for the successful culture of mammalian cells, in both the research and commercial fields. The potential application of albumins, bovine or human serum albumin, for cell culture is a by-product
Tamara Topală et al.
Clujul medical (1957), 87(4), 215-219 (2014-01-01)
The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum
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