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Merck

A3299

Bovine Serum Albumin solution

30% in 0.85% sodium chloride, aseptically filled

Synonym(s):

Albumin solution from bovine serum, BSA solution

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About This Item

CAS Number:
9048-46-8
UNSPSC Code:
12352202
NACRES:
NA.27
MDL number:
MFCD00130384

Key Documents

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Product Name

Bovine Serum Albumin solution, 30% in 0.85% sodium chloride, aseptically filled

biological source

bovine

sterility

aseptically filled

assay

28-32% (biuret)

form

solution

quality

high avidity

purified by

heat shock fractionation

contains

0.1% sodium azide as preservative

does not contain

stabilizer

origin

USA origin

concentration

28-32% (biuret)
30% in 0.85% sodium chloride

UniProt accession no.

P02769

storage temp.

2-8°C

Quality Level

200

Gene Information

bovine ... ALB(280717)

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Application

Bovine Serum Albumin solution has been used as a standard for the quantification of protein in extracellular polymeric substances (EPSs) using the Lowry method.

Analysis Note

High avidity
Tested for avidity with known incomplete antibody (not saline agglutinable).

Biochem/physiol Actions

Bovine Serum Albumin (BSA) facilitates the transport of drugs, hormones, and fatty acids. It is used as a blocking agent in enzyme-linked immunosorbent assay (ELISA). BSA is an important constituent of the cell culture media and favors embryonic stem cells (hESC) differentiation. It plays a vital role in the cosmetic and pharmaceutical industry.

General description

Bovine serum albumin (BSA) is a member of the serum albumin family. It is a globular, α-helical, and non-glycosylated protein. BSA is a single-chain protein and consists of three domains with two sub-domains under each. It has 17-disulfide bonds.

Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter

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Certificates of Analysis (COA)

Lot/Batch Number
SLCH3513
SLCD7366
SLBZ9468
SLBX7377
SLBV6740

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Ultrasound, thermal and alkali treatments affect extracellular polymeric substances (EPSs) and improve waste activated sludge dewatering
Ruiz-Hernando M, et al.
Process Biochemistry (Oxford, United Kingdom), 50(3), 438-446 (2015)
Structural changes during the unfolding of Bovine serum albumin in the presence of urea: A small-angle neutron scattering study
Das A, et al.
Pramana, 63(2), 363-368 (2004)
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
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
Nikolay N Brandt et al.
Journal of biomedical optics, 20(5), 051015-051015 (2014-12-06)
The analysis of the structure-function relationship is extremely important in the study of proteins. The importance of function-related motions of large parts or subglobules of protein molecules stimulates the spectroscopic study in the low-frequency (terahertz) domain. However, only tentative assignments
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