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Key Documents

A5170

Sigma-Aldrich

Anti-Avidin antibody produced in rabbit

whole antiserum

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

whole antiserum

antibody product type

primary antibodies

clone

polyclonal

contains

15 mM sodium azide

technique(s)

immunoelectrophoresis: suitable
indirect ELISA: 1:100,000

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

Avidin is a homotetrameric glycoprotein found in the egg white of birds, reptiles and amphibians. Each subunit is 16 kDa, singly glycosylated and binds to a molecule of biotin with greater affinity and specificity. Recombinant avidin from corn is similar to avidin from egg white in terms of properties like isoelectric point (pI) and antigenic properties. Avidin from corn has low molecular weight than chicken egg-derived avidin. Commercial production of avidin from corn has certain advantages in terms of availability of greater biomass and avoiding the co-purification of animal virus.

Immunogen

avidin

Application

Anti-Avidin antibody produced in rabbit has been used in enzyme-linked immunosorbent assay (ELISA). It has also been used in preparation of antibody-Au nanoparticles.
The presence of Scavidin in BT4C glioma cells was assessed by western blot using a rabbit anti-avidin antibody as the primary at a dilution of 1:4000. Lehtolainen, P. (2002) Cloning and Characterization of Scavidin, a Fusion Protein for the Targeted Delivery of Biotinylated Molecules. J. Biol. Chem. 277:8545-8550.

Biochem/physiol Actions

Avidin 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.

Physical form

Supplied as a liquid containing 15mM sodium azide as preservative

Preparation Note

treated to remove lipoproteins

Analysis Note

This antisera is evaluated for performance and specificity by immunodiffusion and immunoelectrophoresis.

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

10 - Combustible liquids

wgk_germany

nwg

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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Coomassie Brilliant Dyes as Surface-Enhanced Raman Scattering Probes for Protein-Ligand Recognitions
Han, Xiao X. and others
Analytical Chemistry, 82(10), 4102-4106 (2010)
Commercial plant-produced recombinant avidin
Commercial Plant-Produced Recombinant Protein Products, 15-25 (2014)
Development of transgenic wheat (Triticum aestivum L.) expressing avidin gene conferring resistance to stored product insects
Abouseadaa HH, et al.
BMC plant biology, 15(1), 1-8 (2015)
Xiao X Han et al.
Analytical chemistry, 82(10), 4102-4106 (2010-04-24)
Coomassie brilliant dyes have high affinity to proteins and high Raman activity, and on the basis of which, we have employed brilliant blue R-250 (BBR) and brilliant blue G-250 (BBG) as surface-enhanced Raman scattering (SERS) labels to probe protein-ligand recognitions.
Colleen Murray et al.
Transgenic research, 19(6), 1041-1051 (2010-03-11)
The high affinity biotin-binding proteins (BBPs) avidin and streptavidin are established insecticidal agents, effective against a range of insect pests. Earlier work showed that, when expressed in planta, full length avidin and a truncated form of streptavidin are highly insecticidal.

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