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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

UNSPSC Code:
12352202
NACRES:
NA.28

biological source

bovine

Quality Level

100

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

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.

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).

Other Notes

For life science research only. Not for use in diagnostic procedures.
Loss on drying: ≤5.0%

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Osvědčení o analýze (COA)

Vyhledejte osvědčení Osvědčení o analýze (COA) zadáním čísla šarže/dávky těchto produktů. Čísla šarže a dávky lze nalézt na štítku produktu za slovy „Lot“ nebo „Batch“.

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Navštívit knihovnu dokumentů

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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