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关于此项目
NACRES:
NA.28
UNSPSC Code:
12352202
Biological source:
bovine
Assay:
≥98.5%
Form:
lyophilized
Technique(s):
cell culture | stem cell: suitable
Impurities:
<10 ppm Heavy metals
1% Ash
1% Ash
产品名称
BSA Fraction V, ≥98.5%, Ash 1%, Heavy metals < 10 ppm, stem cell culture, Mycoplasma Negative, USA origin
biological source
bovine
assay
≥98.5%
form
lyophilized
mol wt
Mr =68,000
packaging
pkg of 1 kg (03116964001)
pkg of 250 g (03116956001)
manufacturer/tradename
Roche
origin
USA origin
technique(s)
cell culture | stem cell: suitable
impurities
<10 ppm Heavy metals
1% Ash
solubility
≤0.40 (A550)
absorption
≤0.40 at 550 nm
foreign activity
Mycoplasma (Negative)
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Application
Bovine Serum Albumin Fraction V, heat shock has been used for blocking in immunocytochemistry.
Biochem/physiol Actions
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).
General description
Serum Albumin is a major protein found in circulating blood. Albumin is helical in structure with three domains that form a heart-like shape.
Other Notes
For life science research only. Not for use in diagnostic procedures.
Loss on drying: ≤5.0%
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
监管及禁止进口产品
此项目有
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
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
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
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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