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12660

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2

Synonyma:

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2

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Vybrat velikost

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Velikost baleníSkladová položkaDostupnostCena
100 g

K dispozici k odeslání DNESodAreál Kühne+Nagel spol. s r.o.

9 590,00 Kč
1 kg

K dispozici k odeslání DNESodAreál Kühne+Nagel spol. s r.o.

47 400,00 Kč

O této položce

Číslo CAS:
9048-46-8
MDL number:
MFCD00064211
NACRES:
NA.25
UNSPSC Code:
12352202
eCl@ss:
32160409
Assay:
≥96% (SDS-PAGE)
Form:
solid
Impurities:
≤5% Moisture

9 590,00 Kč

K dispozici k odeslání DNESpodrobné informace

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description

Merck USA index - 14, 8468

Quality Level

100

assay

≥96% (SDS-PAGE)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

impurities

≤5% Moisture

color

off-white

solubility

0.15 M sodium chloride: 10 mg/mL

cation traces

heavy metals: ≤50 ppm

shipped in

ambient

storage temp.

2-8°C

General description

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2 is a native fatty acid profile that reflects endogenous lipids. It has a pH in the range of 4.8-5.4 in 150 mM NaCl (1%).
Bovine serum albumin (BSA), a non-glycosylated globular, α-helical protein, belongs to the serum albumin family. It consists of three domains with two sub-domains each and has 17-disulfide bonds.[1][2]

Application

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2 has been used as a blocking agent in western blotting.[3] It has also been used as a component in phosphate-buffered saline (PBS) for diluting secondary antibodies and blocking in immunofluorescence to observe the localization of the Golgi apparatus.[4]

Biochem/physiol Actions

Bovine Serum Albumin (BSA) is the most vital component of cell culture media. It aids in the differentiation of embryonic stem cells (hESC).[5] It plays a key role in the transportation of drugs, hormones, and fatty acids.[1] BSA is used in enzyme-linked immunosorbent assay (ELISA) as a blocking agent.[6]

Preparation Note

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Standard Handling (A)

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Tato položka
A4919A8806126625
Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2

Sigma-Aldrich

12660

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2

Bovine Serum Albumin heat shock fraction, protease free, low endotoxin, suitable for cell culture, pH 7, ≥98%

Sigma-Aldrich

A4919

Bovine Serum Albumin

Bovine Serum Albumin fatty acid free, low endotoxin, lyophilized powder, BioReagent, suitable for cell culture, ≥96% (agarose gel electrophoresis)

Sigma-Aldrich

A8806

Bovine Serum Albumin

Albumin, Bovine Serum, 30% Aqueous Solution, Stabilizer-Free

Sigma-Aldrich

126625

Albumin, Bovine Serum, 30% Aqueous Solution, Stabilizer-Free

assay

≥96% (SDS-PAGE)

assay

≥98%

assay

≥96% (agarose gel electrophoresis)

assay

≥96% (cellulose acetate electrophoresis)

Quality Level

100

Quality Level

200

Quality Level

300

Quality Level

100

form

solid

form

lyophilized powder

form

lyophilized powder

form

liquid

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

impurities

≤5% Moisture

impurities

protease, none detected, ≤1.0 EU/mg endotoxin

impurities

≤0.02% fatty acid (GC), ≤0.1 ng/mg endotoxin

impurities

-

solubility

0.15 M sodium chloride: 10 mg/mL

solubility

water: soluble (40 mg/ml)

solubility

water: soluble (40 mg/ml)

solubility

-

Skladovací třída

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Osvědčení o analýze (COA)

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Anna Eslami et al.
Journal of visualized experiments : JoVE, (44) (2010-12-30)
Western blotting is an analytical technique used to detect specific proteins in a given sample of tissue homogenate or extract. It uses gel electrophoresis to separate native or denatured proteins by the length of the polypeptide (denaturing conditions) or by
Miyu Tsuchiya et al.
Oncology letters, 11(5), 3279-3286 (2016-04-29)
N-glycosylation is a post-translational protein modification with a wide variety of functions. It has been predicted that R-spondin1 (RSPO1) is N-glycosylated, although this remains unknown. The present study identified that RSPO1 was N-glycosylated at Asn137, and that N-glycosylation of RSPO1
S Chodankar et al.
Physical review. E, Statistical, nonlinear, and soft matter physics, 77(3 Pt 1), 031901-031901 (2008-06-04)
Small-angle neutron scattering (SANS) and dynamic light scattering (DLS) have been used to study conformational changes in protein bovine serum albumin (BSA) due to perturbation in its native structure as induced by varying temperature and pressure, and in presence of
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Globální číslo obchodní položky

Skladová položkaGTIN
A8097-10ML04061833391204
12660-1KG04055977222630
12660-100GM04055977222647

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