A5477
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
Conjugate:
alkaline phosphatase conjugate
Clone:
HA-7, monoclonal
Application:
WB
Citations:
5
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
Quality Level
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.
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.
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.
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
Preparation Note
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
10 - Combustible liquids
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Sho Yoshimoto et al.
mAbs, 15(1), 2287250-2287250 (2023-12-04)
PD-1 checkpoint inhibitors have revolutionized the treatment of patients with different cancer histologies including melanoma, renal cell carcinoma, and non-small cell lung carcinoma. However, only a subset of patients show a dramatic clinical response to treatment. Despite intense biomarker discovery
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
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
The HA tag is cleaved and loses immunoreactivity during apoptosis.
Laura Schembri et al.
Nature methods, 4(2), 107-108 (2007-02-01)
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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