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03117332001

Roche

Bovine Serum Albumin Fraction V, protease-free

from bovine serum

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.21

biological source

bovine

Quality Level

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

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.

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.

Quality

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

Other Notes

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

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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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.
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
Jon T Sack et al.
The Journal of general physiology, 142(3), 315-324 (2013-08-14)
A family of 40 mammalian voltage-gated potassium (Kv) channels control membrane excitability in electrically excitable cells. The contribution of individual Kv channel types to electrophysiological signaling has been difficult to assign, as few selective inhibitors exist for individual Kv subunits.
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
Yuhong Xiao et al.
Journal of immunological methods, 384(1-2), 148-151 (2012-06-27)
The enzyme-linked immunosorbent assay (ELISA) is an extremely common and powerful laboratory technique for detecting proteins by antibodies. Researchers frequently use bovine serum albumin (BSA) as a blocking agent to prevent non-specific binding of antigens and antibodies to the microtiter

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