BSAVHS-RO
Roche
BSA Fraction V
≥98.5%, Ash 1%, Heavy metals < 10 ppm, stem cell culture, Mycoplasma Negative, USA origin
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About This Item
Código UNSPSC:
12352202
NACRES:
NA.28
Productos recomendados
origen biológico
bovine
Nivel de calidad
Ensayo
≥98.5%
Formulario
lyophilized
mol peso
Mr =68,000
envase
pkg of 1 kg (03116964001)
pkg of 250 g (03116956001)
fabricante / nombre comercial
Roche
origen
USA origin
técnicas
cell culture | stem cell: suitable
impurezas
<10 ppm Heavy metals
1% Ash
solubilidad
≤0.40 (A550)
Absorción
≤0.40 at 550 nm
actividad extraña
Mycoplasma (Negative)
Condiciones de envío
wet ice
temp. de almacenamiento
2-8°C
Descripción general
Serum Albumin is a major protein found in circulating blood. Albumin is helical in structure with three domains that form a heart-like shape.
Aplicación
Bovine Serum Albumin Fraction V, heat shock has been used for blocking in immunocytochemistry.
Acciones bioquímicas o fisiológicas
Serum Albumin participates in maintaining the osmotic pressure and pH of the blood. It also participates in the transport of various endogenous and exogenous compounds such as amino acids, drugs, steroids, and fatty acids. Bovine serum albumin (BSA) is applicable as a molecular-weight standard, in vaccine preparation and enzyme-linked immunosorbent assay (ELISA).
Otras notas
For life science research only. Not for use in diagnostic procedures.
Loss on drying: ≤5.0%
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Los clientes también vieron
A K Wright et al.
Biophysical journal, 15(2 Pt 1), 137-141 (1975-02-01)
Birefringence relaxation studies on bovine serum albumin (BSA) reveal transient decay described by a double exponential process. The values of the relaxation times lead to estimation of the size of the equivalent ellipsoid of revolution for BSA. Previous measurements of
Anna Bujacz
Acta crystallographica. Section D, Biological crystallography, 68(Pt 10), 1278-1289 (2012-09-21)
Serum albumin first appeared in early vertebrates and is present in the plasma of all mammals. Its canonical structure supported by a conserved set of disulfide bridges is maintained in all mammalian serum albumins and any changes in sequence are
Bill X Huang et al.
Journal of the American Society for Mass Spectrometry, 15(8), 1237-1247 (2004-07-28)
Serum albumin is the principal transporter of fatty acids that are otherwise insoluble in circulating plasma. While the crystal structure of human serum albumin (HSA) as well as its binding with fatty acids has been characterized, the three dimensional structure
Aindrila Chatterjee et al.
Cell, 167(3), 722-738 (2016-10-22)
A functional crosstalk between epigenetic regulators and metabolic control could provide a mechanism to adapt cellular responses to environmental cues. We report that the well-known nuclear MYST family acetyl transferase MOF and a subset of its non-specific lethal complex partners
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