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A5477

Sigma-Aldrich

Anticorps monoclonal Anti-HA

clone HA-7, purified from hybridoma cell culture

Synonyme(s) :

Anti-HA, Anti-hémagglutinine de la grippe

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.56

Source biologique

mouse

Conjugué

alkaline phosphatase conjugate

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

HA-7, monoclonal

Forme

buffered aqueous glycerol solution

Technique(s)

western blot: 1:4,000 using extracts of mammalian cells expressing HA tagged fusion proteins

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Description générale

Monoclonal anti-HA, Alkaline Phosphatase conjugate is derived from the HA-7 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice, immunized with a synthetic peptide. Human influenza hemagglutinin (HA), a surface glycoprotein exists as a trimer. The monomeric HA comprises base and membrane distal-tip regions with conserved residues and receptor-binding site, respectively.

Spécificité

L′anticorps reconnaît tant les formes natives que dénaturées et réduites des protéines de fusion avec une étiquette HA. Il réagit avec les protéines de fusion exprimées dans E. coli ou dans les cellules de mammifères et dont l′étiquette HA se situe à l′extrémité N-terminale ou C-terminale.

Immunogène

Peptide synthétique correspondant à un fragment de l′hémagglutinine (HA) du virus de la grippe humain, connu sous le nom d′étiquette HA ou HA-tag, conjugué à KLH.

Application

Monoclonal Anti-HA−Alkaline Phosphatase antibody produced in mouse has been used in immunoblotting

Actions biochimiques/physiologiques

Human influenza hemagglutinin (HA) is required for the infectivity of the human virus. HA interacts with the host cell surface glycoproteins especially the sialic acid to initiate infection. The short sequence derived from the HA molecule corresponding to amino acids 98-106 (YPYDVPDYA) has been used as a tag, known as HA-Tag. This tag facilitates the detection, isolation, purification, coprecipitation of proteins and immunostaining proteins. Caspase 3/7 effectively cleaves HA-tag. Many recombinant proteins or protein of interest have been engineered to express the HA tag fusion protein. The HA-tag does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein.

Forme physique

Solution in 0.05 M Tris buffer, pH 8.0, containing 1% BSA, 1 mM MgCl2, 50% glycerol, and 15 mM sodium azide as a preservative

Stockage et stabilité

For continuous use and extended storage, store at 2-8 °C. Do not freeze. Working dilution samples should be discarded if not used within 12 hours.

Clause de non-responsabilité

Unless otherwise stated in our catalog, 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

10 - Combustible liquids


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Consulter la Bibliothèque de documents

Sho Yoshimoto et al.
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Patrick R Arsenault et al.
Molecular and cellular biology, 36(18), 2328-2343 (2016-06-22)
Prolyl hydroxylase domain protein 2 (PHD2) (also known as EGLN1) is a key oxygen sensor in mammals that posttranslationally modifies hypoxia-inducible factor α (HIF-α) and targets it for degradation. In addition to its catalytic domain, PHD2 contains an evolutionarily conserved
The HA tag is cleaved and loses immunoreactivity during apoptosis.
Laura Schembri et al.
Nature methods, 4(2), 107-108 (2007-02-01)
Steven J Gamblin et al.
The Journal of biological chemistry, 285(37), 28403-28409 (2010-06-12)
Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus with their common ligand/substrate: carbohydrate chains terminating in sialic acid. The specificity of virus attachment to target
Hansjörg Götzke et al.
Nature communications, 10(1), 4403-4403 (2019-09-29)
Specialized epitope tags are widely used for detecting, manipulating or purifying proteins, but often their versatility is limited. Here, we introduce the ALFA-tag, a rationally designed epitope tag that serves a remarkably broad spectrum of applications in life sciences while

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