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HA antibody is a good substitute for the 12CA5 monoclonal antibody.
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Expression. With this technique, gene expression can end up easily monitored on traditional western blotting, immunoprecipitation and immunofluorescence thanks to an antibody that recognizes this epitope. Amino acid sequences which were widely used for epitope tagging are as follow; YPYDVPDYA (HA-Tag), EQKLISEEDL (Myc-Tag) together with YTDIEMNRLGK (VSV-G-Tag), which match the partial peptide with Influenza hemagglutinin protein, the Human c-myc gene product and also the Vesicular stomatitis virus glycoprotein respectively.
Monoclonal antibody HAYA. 11 (HA, 16B12, flu tag) was raised against the twelve amino chemical p peptide CYPYDVPDYASL. This second-generation
HA antibody is a good substitute for the 12CA5 monoclonal Anti-SMAD3,Anti-Desmin Antibody,HA Antibody antibody. HAYA. 11 recognizes the influenza hemagglutinin epitope
(YPYDVPDYA) that's been used extensively for a general epitope tag with expression vectors. The extreme specificity of the antibody allows
unambiguous identification and quantitative analysis of the tagged protein. The HA. 11 antibody recognizes HA epitopes located during
protein sequences as well as at the N- or C-terminus.
95% homogeneity as a result of standard chromatographic techniques.
Anti-HA is developed in rabbit which has a synthetic peptide
corresponding to help amino acid residues 98-106 (Tyr-Pro-
Tyr-Asp-Val-Pro-Asp-Tyr-Ala) of the human Influenza
hemagglutinin (HA), conjugated to KLH. This antibody is
affinity-purified on the immobilized immunizing peptideAnti-HA can be utilized for immunoblotting of recombinant
proteins tagged with HA at the amino or carboxy
terminus. This antibody may recognize cross-reacting
bands in certain mammalian cells. Staining in the fusion
protein band is specifically inhibited with the immunizing
HA peptide (Product or service No. I 2149). The antibody is usually
useful for detection with HA-tagged fusion proteins just by
immunoprecipitation and by immunofluorescent yellowing
of transfected cells.
Recombinant DNA technological know-how enables the attachment
involving genes of interest to help specific sequences or family genes,
which can provide 'affinity handles' (tags) that will
enable the selective identification and purification with the
protein of interest. 1-6 The addition of an tag to a given
gene creates a stable fusion product that does not
appear to interfere while using the bioactivity of the health proteins, or
with the biodistribution with the tagged product.
Influenza hemagglutinin protein is a nonapeptide
derived from this major spike membrane glycoprotein with
the human influenza virus. This strain specific
glycoprotein is a homotrimer of 84 kDa monomers,
just about every containing two disulfide-linked subunits: HA1 together with
HA2. The nucleic acid sequence encoding the HApeptide
has been incorporated into various expression
plasmids adjacent to this cloning site thus allowing the
cloning and phrase of HA-tagged fusion healthy proteins.
Such fusion proteins may very well be expressed in cells with
various organisms: bacteria, get rid of, insects and
mammals. Inside fusion protein, the HA sequence may
serve for a recognition target for certain antibodies thus
enabling recognition, subcellular localization, characterization,
quantification, practicable analysis and affinity
purification with the HA-tagged protein and linked
bound proteins. 4.
Monoclonal antibody HAYA. 11 (HA, 16B12, flu tag) was raised against the twelve amino chemical p peptide CYPYDVPDYASL. This second-generation
HA antibody is a good substitute for the 12CA5 monoclonal Anti-SMAD3,Anti-Desmin Antibody,HA Antibody antibody. HAYA. 11 recognizes the influenza hemagglutinin epitope
(YPYDVPDYA) that's been used extensively for a general epitope tag with expression vectors. The extreme specificity of the antibody allows
unambiguous identification and quantitative analysis of the tagged protein. The HA. 11 antibody recognizes HA epitopes located during
protein sequences as well as at the N- or C-terminus.
95% homogeneity as a result of standard chromatographic techniques.
Anti-HA is developed in rabbit which has a synthetic peptide
corresponding to help amino acid residues 98-106 (Tyr-Pro-
Tyr-Asp-Val-Pro-Asp-Tyr-Ala) of the human Influenza
hemagglutinin (HA), conjugated to KLH. This antibody is
affinity-purified on the immobilized immunizing peptideAnti-HA can be utilized for immunoblotting of recombinant
proteins tagged with HA at the amino or carboxy
terminus. This antibody may recognize cross-reacting
bands in certain mammalian cells. Staining in the fusion
protein band is specifically inhibited with the immunizing
HA peptide (Product or service No. I 2149). The antibody is usually
useful for detection with HA-tagged fusion proteins just by
immunoprecipitation and by immunofluorescent yellowing
of transfected cells.
Recombinant DNA technological know-how enables the attachment
involving genes of interest to help specific sequences or family genes,
which can provide 'affinity handles' (tags) that will
enable the selective identification and purification with the
protein of interest. 1-6 The addition of an tag to a given
gene creates a stable fusion product that does not
appear to interfere while using the bioactivity of the health proteins, or
with the biodistribution with the tagged product.
Influenza hemagglutinin protein is a nonapeptide
derived from this major spike membrane glycoprotein with
the human influenza virus. This strain specific
glycoprotein is a homotrimer of 84 kDa monomers,
just about every containing two disulfide-linked subunits: HA1 together with
HA2. The nucleic acid sequence encoding the HApeptide
has been incorporated into various expression
plasmids adjacent to this cloning site thus allowing the
cloning and phrase of HA-tagged fusion healthy proteins.
Such fusion proteins may very well be expressed in cells with
various organisms: bacteria, get rid of, insects and
mammals. Inside fusion protein, the HA sequence may
serve for a recognition target for certain antibodies thus
enabling recognition, subcellular localization, characterization,
quantification, practicable analysis and affinity
purification with the HA-tagged protein and linked
bound proteins. 4.
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