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P3775

Sigma-Aldrich

Anti-Protein A antibody produced in rabbit

fractionated antiserum, lyophilized powder

Synonyme(s) :

Anti-Protein A

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

fractionated antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

lyophilized powder

Conditionnement

vial of 2 mL lyophilized antiserum

Technique(s)

indirect ELISA: 1:100,000

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Catégories apparentées

Description générale

Protein A is a 42 kDa bacterial protein. It is isolated from the cell wall of Staphylococcus aureus.
The fractionation procedure yields primarily the immunoglobulin fraction of antiserum. To ensure specificity the fractionated antiserum is adsorbed using solid phase techniques, if necessary. Rabbit Anti-Protein A is lyophilized from 0.01 M phosphate buffered saline, pH 7.2, to which no preservatives have been added. Identity and purity of the antibody is established by immunoelectrophoresis. Electrophoresis of the antibody preparation followed by diffusion versus anti-rabbit IgG results in a single arc of precipitation and versus anti-rabbit whole serum results in multiple arcs of precipitation.

Immunogène

Protein A from Staphylococcus aureus

Application

Anti-Protein A antibody produced in rabbit has been used in immunoblotting.
Protein A may be used as in immunoblotting with a minimum dilution of 1:50,000.

Actions biochimiques/physiologiques

Protein A has an ability to bind Fc region of immunoglobulins from several species. It is used as a “universal tracer” and it facilitate the segregation of bound and free ligand. Protein A also acts as affinity matrices for antibody (IgG) purification.

Forme physique

Lyophilized from 0.01M phosphate buffered saline, pH 7.2

Reconstitution

Reconstitute with 2 ml deionized water.

Clause de non-responsabilité

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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Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Smriti Kala et al.
PloS one, 7(10), e46864-e46864 (2012-10-12)
Most mitochondrial mRNAs in trypanosomatid parasites require uridine insertion/deletion RNA editing, a process mediated by guide RNA (gRNA) and catalyzed by multi-protein complexes called editosomes. The six oligonucleotide/oligosaccharide binding (OB)-fold proteins (KREPA1-A6), are a part of the common core of
Ritu Gupta et al.
PloS one, 10(7), e0132350-e0132350 (2015-07-07)
Saccharomyces cerevisiae Sub1 is involved in several cellular processes such as, transcription initiation, elongation, mRNA processing and DNA repair. It has also been reported to provide cellular resistance during conditions of oxidative DNA damage and osmotic stress. Here, we report
Regulation of yeast G protein signaling by the kinases that activate the AMPK homolog Snf1
Clement ST, et al.
Science Signaling, 6(291), ra78-ra78 (2013)
Shintaro Kira et al.
Autophagy, 10(9), 1565-1578 (2014-07-22)
Autophagy is an intracellular degradation process that delivers cytosolic material to lysosomes and vacuoles. To investigate the mechanisms that regulate autophagy, we performed a genome-wide screen using a yeast deletion-mutant collection, and found that Npr2 and Npr3 mutants were defective
Cell cycle-dependent phosphorylation and ubiquitination of a G protein alpha subunit
Torres MP, et al.
The Journal of Biological Chemistry, 286(23), 20208-20216 (2011)

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