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A5477

Sigma-Aldrich

Anti-HA−Alkaline Phosphatase antibody, Mouse monoclonal

clone HA-7, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-HA, Monoclonal Anti-HA−Alkaline Phosphatase antibody produced in mouse, Anti-HA, Anti-Influenza Hemagglutinin

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.56

biological source

mouse

conjugate

alkaline phosphatase conjugate

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

HA-7, monoclonal

form

buffered aqueous glycerol solution

technique(s)

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

shipped in

wet ice

storage temp.

2-8°C

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General description

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.

Specificity

The antibody recognizes native as well as denatured-reduced forms of HA-tagged proteins and is reactive with N- or C-terminal HA-tagged fusion proteins expressed in E. coli or in mammalian cells.

Immunogen

synthetic peptide corresponding to a fragment of human influenza virus hemagglutinin (HA) known as HA-tag, conjugated to KLH

Application

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

Biochem/physiol Actions

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.

Physical form

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

Storage and Stability

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.

Disclaimer

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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Storage Class Code

10 - Combustible liquids


Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

A5477-BULK:
A5477-VAR:
A5477-500UG:


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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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
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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