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Merck
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Documentos clave

126575

Sigma-Aldrich

Albumin, Bovine Serum, Fraction V, Fatty Acid-Free

Sinónimos:

Albumin, Bovine Serum, Fraction V, Fatty Acid-Free

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About This Item

Número de CAS:
9048-46-8
Número MDL:
MFCD00797675
Código UNSPSC:
12352202
NACRES:
NA.25

Ensayo

≥95% (cellulose acetate electrophoresis)

Formulario

powder

fabricante / nombre comercial

Calbiochem®

condiciones de almacenamiento

OK to freeze

impurezas

≤0.02% fatty acids
≤3% ash
≤5% moisture

color

white to light yellow
light yellow to light brown

Condiciones de envío

ambient

temp. de almacenamiento

2-8°C

Descripción general

Albumin, Bovine Serum, (BSA) Fraction V, Fatty Acid-Free is useful for immunodiagnostic assays. It is designed for use in serological testing, radioimmunoassay, and hormone response studies. It is also applicable in binding and transport studies. BSA is prepared by cold ethanol extraction (Cohn method) with a pH: 6.8-7.4.
Bovine serum albumin (BSA) is a non-glycosylated globular, α-helical protein belonging to the serum albumin family. It consists of three domains with two sub-domains each and has 17-disulfide bonds.

Aplicación

Albumin, Bovine Serum, Fraction V, Fatty Acid-Free has been used:
  • as a component of: blocking buffer immunoelectron microscopy (IEM) for various cells
  • mitochondrial isolation buffer (MIB) and mitochondria assay solution (MAS) to trap free fatty acids released during adipose tissue homogenization
  • blocking buffer for wholemount staining of the esophageal epithelium (EE) in immunofluorescence

Acciones bioquímicas o fisiológicas

Bovine Serum Albumin (BSA), the most vital component of cell culture media, aids in embryonic stem cells (hESC) differentiation. It aids the transportation of drugs, hormones, and fatty acids. BSA is also used as a blocking agent in enzyme-linked immunosorbent assay (ELISA).

Advertencia

Toxicity: Standard Handling (A)

Nota de preparación

May take up to 24 h to fully dissolve.

Reconstitución

Following reconstitution, store in the refrigerator (4°C). 0.1% NaN₃ may be added as a preservative. Stock solutions are stable for up to 3 months at 4°C.

Información legal

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

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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M Prats
European journal of biochemistry, 75(2), 619-625 (1977-05-16)
The L-(+)-Lactate:cytochrome c oxidoreductase or cytochrome b2 from the yeasts Saccharomyces cerevisiae and Hansenula anomala were partially hydrolysed in various concentrations of trypsin. Conditions were found which allowed the isolation from the Hansenula enzyme of a 140 000 +/- 10
Andrew W Ferree et al.
Autophagy, 9(11), 1887-1896 (2013-10-24)
To study mitochondrial protein age dynamics, we targeted a time-sensitive fluorescent protein, MitoTimer, to the mitochondrial matrix. Mitochondrial age was revealed by the integrated portions of young (green) and old (red) MitoTimer protein. Mitochondrial protein age was dependent on turnover
E Sandra Chocron et al.
Molecular endocrinology (Baltimore, Md.), 26(7), 1117-1128 (2012-05-10)
We previously demonstrated that the thyroid hormone, T(3), acutely stimulates mitochondrial metabolism in a thyroid hormone receptor (TR)-dependent manner. T(3) has also recently been shown to stimulate mitochondrial fatty acid oxidation (FAO). Here we report that TR-dependent stimulation of metabolism
Jacob M Serfass et al.
The Journal of biological chemistry, 292(24), 10097-10111 (2017-04-30)
Endocytosis, and the subsequent trafficking of endosomes, requires dynamic physical alterations in membrane shape that are mediated in part by endophilin proteins. The endophilin B family of proteins contains an N-terminal Bin/amphiphysin/Rvs (N-BAR) domain that induces membrane curvature to regulate
Mohyeddine Omrane et al.
iScience, 13, 138-153 (2019-03-05)
Septins are GTP-binding proteins involved in several membrane remodeling mechanisms. They associate with membranes, presumably using a polybasic domain (PB1) that interacts with phosphoinositides (PIs). Membrane-bound septins assemble into microscopic structures that regulate membrane shape. How septins interact with PIs
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