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Merck

B1520

Anti-Bovine Albumin antibody produced in rabbit

whole antiserum

Synonym(s):

Anti-Albumin, bovine serum (BSA)

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:

Product Name

Anti-Bovine Albumin antibody produced in rabbit, whole antiserum

biological source

rabbit

conjugate

unconjugated

antibody form

whole antiserum

antibody product type

primary antibodies

clone

polyclonal

contains

15 mM sodium azide

species reactivity

bovine

technique(s)

indirect ELISA: 1:200,000
quantitative precipitin assay: 3.0 mg/mL

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

bovine ... Alb(280717)

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Application

Anti-Bovine Albumin antibody produced in rabbit may be used for ELISA at a working dilution of 1:200,000. The antibody was used for in vitro labeling of albumin present in mammary tissue extract of lactating cow.
It has also been used for the detection of albumin in nanoparticle using scanning transmission electron microscope.

Biochem/physiol Actions

Albumin is the most abundant circulating proteins present in the serum that binds and transports long-chain fatty acid anions, detoxifies unconjugated bilirubin and transports thyroid and steroid hormones.
Human serum albumin as a transporter, is considered as drug delivery vehicle for treating human diseases. Post-translational modifications like glycation and cysteinylation affects the binding functionality of serum albumin. High albumin protein diet has influence on hyperalbuminemia. Low levels of albumin leads to hypoalbuminemia, associated with decreased production and distribution. Hypoalbuminemia is a risk factor for the development of cardiovascular disease.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Serum albumin in humans is encoded by the gene mapped to human chromosome 4q13.3. Serum albumin is one of the abundant proteins in the blood and has a molecular weight of 66 kDa.
Anti-Bovine Serum Albumin (BSA) was developed in rabbit using purified BSA from Cohn Fraction V as the immunogen. The antiserum has been treated to remove lipoproteins. Strong reactivity with BSA has been determined by immunoelectrophoresis (IEP).

Physical form

Rabbit Anti-BSA is provided as a liquid containing 15 mM sodium azide as preservative.

Preparation Note

For continuous use, store at 2-8 °C for up to one month. For extended storage, the solution may be frozen in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Miachael Karl et al.
European journal of biochemistry, 270(7), 1536-1542 (2003-03-26)
The nuclei in the plasmodium of Physarum polycephalum, as of other myxomycetes, contain high amounts of polymalate, which has been proposed to function as a scaffold for the carriage and storage of several DNA-binding proteins [Angerer, B. and Holler, E.
Unraveling the mysteries of serum albumin?more than just a serum protein.
Merlot AM, et al.
Frontiers in Physiology, 5, 299-299 (2014)
Pedram Madadkar et al.
Journal of pharmaceutical analysis, 8(3), 187-193 (2018-06-21)
Enrichment and immobilization of analytes by chemical bonding or physical adsorption is typically the first step in many commonly used analytical techniques. In this paper, we discuss a permeation drag based technique as an alternative approach for carrying out location-specific
Association of serum albumin and atherosclerosis in chronic hemodialysis patients.
Beddhu S, et al.
American Journal of Kidney Diseases, 40(4), 721-727 (2002)
Modifications of human serum albumin and their binding effect.
Lee P and Wu X
Current Pharmaceutical Design, 21(14), 1862-1865 (2015)

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