Skip to Content
Merck

03117332001

Roche

Bovine Serum Albumin Fraction V, protease-free

from bovine serum

Sign In to View Organizational & Contract Pricing.

Select a Size



About This Item

NACRES:
NA.21
UNSPSC Code:
12352202

Product Name

Bovine Serum Albumin Fraction V, protease-free, from bovine serum

biological source

bovine

assay

≥98.5% albumin basis (electrophoresis)

form

lyophilized

packaging

pkg of 50 g

manufacturer/tradename

Roche

technique(s)

ELISA: suitable

shipped in

wet ice

storage temp.

2-8°C

Quality Level

Analysis Note

Contaminants: ≤0.001% heavy metals; proteases not detectable (casein digest)

Application

Bovine Serum Albumin Fraction V, protease-free is used:
  • for stabilization of purified enzymes
  • for site-blocking reagent in ELISA techniques
  • as a protein standard for determination of protein concentration

Biochem/physiol Actions

Bovine Serum Albumin (BSA) facilitates the transmission of drugs, hormones, and fatty acids. It is the most commonly used blocking agent in enzyme-linked immunosorbent assay (ELISA). BSA enhances the differentiation of human embryonic stem cells (hESC) and is also a chief component of cell culture media.

General description

Bovine serum albumin (BSA) is a globular, α-helical, non-glycosylated protein is produced in the liver. It consists of three homologous, structurally different domains and two sub-domains each. BSA has 17 cysteine residues cross-linked and bound into a single chain.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Drew C Tilley et al.
The Journal of general physiology, 151(3), 292-315 (2018-11-07)
Allosteric ligands modulate protein activity by altering the energy landscape of conformational space in ligand-protein complexes. Here we investigate how ligand binding to a K+ channel's voltage sensor allosterically modulates opening of its K+-conductive pore. The tarantula venom peptide guangxitoxin-1E
Amanda B Hummon et al.
BioTechniques, 42(4), 467-470 (2007-05-11)
A systems approach is being applied in many areas of the biological sciences, particularly in cancer research. The coordinated, simultaneous extraction of DNA, RNA, and proteins from a single sample is crucial for accurate correlations between genomic aberrations and their
Glennys V Reynoso et al.
Methods in molecular biology (Clifton, N.J.), 2023, 287-299 (2019-06-27)
This chapter provides methods for the propagation, purification, and titration of vaccinia virus (VACV) and the highly attenuated strain-modified vaccinia Ankara (MVA). Additionally, we provide information on VACV recombinants we have used for intravital imaging with multiphoton excitation.
D J Speca et al.
Genes, brain, and behavior, 13(4), 394-408 (2014-02-06)
The Kv2.1 delayed rectifier potassium channel exhibits high-level expression in both principal and inhibitory neurons throughout the central nervous system, including prominent expression in hippocampal neurons. Studies of in vitro preparations suggest that Kv2.1 is a key yet conditional regulator
Xinghui Tian et al.
Methods in molecular biology (Clifton, N.J.), 430, 119-133 (2008-03-29)
The successful isolation and characterization of human embryonic stem cells (hESCs) provides a powerful tool to study the cellular and genetic mechanisms that mediate cell-fate decisions toward distinct developmental lineages. hESC-derived cells may also be suitable for novel cellular therapies.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service