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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

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 Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
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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