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Merck

A5170

Sigma-Aldrich

Anti-Avidin antibody produced in rabbit

whole antiserum

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.43

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

whole antiserum

tipo de anticuerpo

primary antibodies

clon

polyclonal

contiene

15 mM sodium azide

técnicas

immunoelectrophoresis: suitable
indirect ELISA: 1:100,000

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Descripción general

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.

Inmunógeno

avidin

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Forma física

Supplied as a liquid containing 15mM sodium azide as preservative

Nota de preparación

treated to remove lipoproteins

Nota de análisis

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

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

nwg

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «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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