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A7419

Sigma-Aldrich

Avidin–Peroxidase

buffered aqueous solution

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Synonym(s):
Avidin–HRP
MDL number:
NACRES:
NA.46

biological source

avidin from egg white
enzyme from horseradish

conjugate

peroxidase conjugate

form

buffered aqueous solution

technique(s)

indirect ELISA: 1:100,000
western blot: 1:400,000-1:800,000 using detecting β-Actin in total cell extract of HeLa cells (5-10 μg/well)

shipped in

dry ice

storage temp.

−20°C

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This Item
A3151A7294A5170
vibrant-m

A7419

Avidin–Peroxidase

vibrant-m

A3151

Avidin–Peroxidase

vibrant-m

A7294

Avidin–Alkaline Phosphatase

biological source

avidin from egg white, enzyme from horseradish

biological source

avidin from egg white, enzyme from horseradish

biological source

avidin from egg white, enzyme from bovine (calf) intestine

biological source

rabbit

form

buffered aqueous solution

form

lyophilized powder

form

buffered aqueous solution

form

-

conjugate

peroxidase conjugate

conjugate

peroxidase conjugate

conjugate

alkaline phosphatase conjugate

conjugate

unconjugated

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

Avidin is homotetrameric protein (68kDa) obtained from egg whites and binds strongly to biotin. Thus, avidin-biotin association has been utilized in immunoassays to detect the localization of antigens in tissues. The use of avidin-biotin immunoassay enhances the sensitivity of the technique and facilitates the detection of antigens in low quantities.

Application

Avidin-Peroxidase has been used for ELISA applications. The product can also be used for western blot applications at dilutions ranging from 1:400,000 to 1:800,000.
Western blot analysis of proteins in HUVEC cells that had underwent cell surface biotinylation were detected using HRP-conjugated avidin at 33.3 ng/ml.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.

Preparation Note

Affinity purified protein.

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.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Prajna Lalitha et al.
American journal of ophthalmology, 144(4), 552-556 (2007-08-19)
To study the range of ocular symptoms in a cohort of patients with chikungunya infection. Retrospective, observational case series. Patients attending a tertiary eye care hospital in South India were included in the study. We included adult patients with serologically
Erica A Peterson et al.
Journal of cell science, 116(Pt 12), 2399-2408 (2003-05-02)
Cell-surface annexin 2 (A2) and its ligand p11 have been implicated in fibrinolysis because of their ability to accelerate tissue plasminogen activator (tPA)-mediated activation of plasminogen to plasmin. Because thrombin is a potent cell modulator obligately produced at the site
Akitoshi Hasegawa et al.
American journal of obstetrics and gynecology, 192(4), 1038-1043 (2005-04-23)
Lactoferrin, an iron-binding glycoprotein found in cervical mucus and amniotic fluid, plays a defensive role against mucosal infections. This study examined the effect of recombinant human lactoferrin on preterm delivery in a rabbit model. Anesthetized rabbits were randomly assigned to
Dominika Lukas et al.
Proceedings of the National Academy of Sciences of the United States of America, 114(8), E1480-E1489 (2017-02-09)
TGF-β is an anti-inflammatory cytokine whose signaling is negatively controlled by Smad7. Previously, we established a role for Smad7 in the generation of autoreactive T cells; however, the function of Smad7 in dendritic cells (DCs) remains elusive. Here, we demonstrate
J J Quinlan et al.
Applied and environmental microbiology, 63(2), 482-487 (1997-02-01)
Five monoclonal antibodies against bacterial spores of Bacillus cereus T and Clostridium sporogenes PA3679 were developed. Two antibodies (B48 and B183) were selected for their reactivity with B. cereus T spores, two (C33 and C225) were selected for their reactivity

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