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SAB5300168

Sigma-Aldrich

Monoclonal Anti-HRP antibody produced in mouse

clone 3A5C6, ascites fluid

Synonym(s):

Anti-Hrp Antibody, Anti-Hrp Antibody - Monoclonal Anti-HRP antibody produced in mouse, N/A

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

3A5C6, monoclonal

technique(s)

direct ELISA: 1:10,000
western blot: 1:500-1:2,000

isotype

IgG1

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

Horseradish peroxidase (HRP) is a heme-containing enzyme. In the presence of hydrogen peroxide, the enzyme catalyzes the oxidation of luminol.

Immunogen

Purified recombinant fragment of HRP expressed in E.coli.
Mouse monoclonal antibody raised against HRP

Physical form

Ascitic fluid containing 0.03% sodium azide.

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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International journal of molecular sciences, 25(13) (2024-07-13)
Secretory IgA (SIgA) presents a promising avenue for mucosal immunotherapy yet faces challenges in expression, purification, and stability. IgA exists in two primary isotypes, IgA1 and IgA2, with IgA2 further subdivided into two common allotypes: IgA2m(1) and IgA2m(2). The major
Horseradish peroxidase: a modern view of a classic enzyme
Veitch NC, et al.
Phytochemistry, 65(3), 249-259 (2004)
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