Saltar al contenido
Merck

03117332001

Roche

Bovine Serum Albumin Fraction V, protease-free

from bovine serum

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

UNSPSC Code:
12352200

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

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

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.
Tamara Topală et al.
Clujul medical (1957), 87(4), 215-219 (2014-01-01)
The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum
Anna Lidia Wojdała et al.
Journal of Alzheimer's disease : JAD, 88(4), 1459-1468 (2022-07-06)
Phosphatidylethanolamine binding protein 1 (PEBP1) is a multifunctional protein, mainly known for its specific binding of phosphatidylethanolamine and the ability to suppress the Raf1-MAPK pathway. Its potential role as an Alzheimer's disease (AD) biomarker has been proposed in several studies.

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico