The hemagglutinin (HA) gene is mapped to segment 4 of Influenza B viral genome. HA is a dominant antigen present on the influenza viral surface. HA is a homotrimer, in which each monomer is produced as a single polypeptide. This monomer is cleaved into two subunits HA1 and HA2 by the host protease.
Influenza hemagglutinin protein is a nonapeptide derived from the major spike membrane glycoprotein of the human influenza virus. This strain specific glycoprotein is a homotrimer of 84 kDa monomers. Each monomers contain two disulfide-linked subunits: HA1 and HA2.
Anti-HA is produced in rabbit using a synthetic peptide corresponding to amino acid residues of the human Influenza hemagglutinin (HA), conjugated to KLH. The antibody is affinity-purified on the immobilized immunizing peptide.
Anti-HA antibody is specific for N- or C-terminal HA-tagged fusion proteins. The product may detect cross-reacting bands in certain mammalian cells. The immunizing HA peptide (Product No.I2149) specifically inhibits the staining of the HA-tagged protein band.
Anti-HA antibody is specific for N- or C-terminal HA-tagged fusion proteins.
The antibody reacts specifically with HA-tagged fusion proteins by immunoblotting and immunoprecipitation.
Synthetic peptide corresponding to amino acid residues of human Influenza virus hemagglutinin (HA) known as HA-tag, conjugated to KLH.
Anti-HA antibody is suitable for use in immunoprecipitation and western blot.
It is also suitable for indirect immunofluorescence (10-20μg/mL using HA-tagged fusion protein transfected cells), immunoprecipitation (2.5-4μg/test using HA-tagged fusion protein from cell lysates), and western blot (0.5-0.8μg/mL using HA-tagged fusion protein transfected cell extracts).
0.2, 0.5 mL
Hemagglutinin (HA) is an influenza-virus glycoprotein that regulates membrane fusion and receptor-binding functions during viral entry and infection. The virus gain entry into the host cell via endocytosis and successive membrane fusion mediated by the HA antigen. HA plays a crucial role in viral pathogenesis and host response to viral infection.
The HA gene is often used as an affinity tag for target proteins in recombinant expression vector systems. The HA-tagged proteins produced from such systems yield stable fusion products that do not interfere with the function and distribution of target proteins. Anti-HA antibody may detect cross-reacting bands in certain mammalian cells. The immunizing HA peptide (Product No.I2149) specifically inhibits the staining of the HA-tagged protein band. The nucleic acid sequence encoding the HA peptide has been incorporated into various expression plasmids adjacent to the cloning site thus enabling the cloning and expression of HA-tagged fusion protein. Such fusion proteins may be expressed in cells of various organisms: bacteria, yeast, insects and mammals. In the fusion protein, the HA sequence may serve as a recognition target for specific antibodies thus enabling detection, subcellular localization, characterization, quantification, functional analysis and affinity purification of the HA-tagged protein and associated bound proteins. Insertion of the HA epitope in different regions of a cellular protein followed by examination of the immunoreactivity of the epitope in intact and in permeabilized cells is useful for studying the cellular expression levels, topology and functional activity of the tagged protein. Antibody mediated detection of the HA tag obviates the need for time consuming generation of antibody specific for newly identified, low abundance, unstable, difficult to purify, cross-reactive or poorly immunogenic proteins.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide
Storage and Stability
For continuous use, store at 2-8 °C for up to one month.
For extended storage freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Solutions at working dilution should be discarded if not used within 12 hours.
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.