92000-76-5 Usage
Uses
Influenza Hemagglutinin (HA) Peptide may be used in immunoblotting. It may also be used to to elute HA-tagged fusion proteins from an affinity column of Monoclonal Anti-HA agarose.
General Description
Influenza Hemagglutinin (HA) peptide is a synthetic peptide with an amino acid sequence of N-Tyr-Pro-Tyr-Asp-Val-Pro-Asp-Tyr-Ala-C. This corresponds to amino acids 98-106 of the human influenza virus hemagglutinin. The HA Peptide is used for competing out the anti-HA antibody binding to HA-tagged fusion proteins in immunoassays. The successful inhibition of antibody binding by HA peptide demonstrates binding is specific.
Biological Activity
ha tag,complexes containing plasmid dna, transferrin-polylysine conjugates, and polylysine-conjugated peptides derived from the n-terminal sequence of the influenza virus hemagglutinin subunit ha-2 have been used for the transfer of luciferase or -galactosidase marker genes to k562 cells, hela cells, and bnl cl.2 hepatocytes. the presence of these influenza peptide conjugates in the dna complexes renders the complexes active in membrane disruption in a liposome leakage assay and results in a substantial augmentation of the transferrin-polylysine-mediated gene transfer.fusogenic peptides derived from the n-terminal sequence of the influenza virus hemagglutinin subunit ha-2 is part of the dna complexes and the resulting augmentation of gene transfer to cultured cells1.in the influenza virus, the hemagglutinin (ha) protein mediates both binding of the virus to the cell surface and the subsequent fusion of viral and cellular membranes. ha is composed of a receptor-binding subunit, denoted ha1, and a fusogenic subunit, denoted ha2. the native ha1yha2 complex, as found on the surface of the native virus, is fusioninactive. for influenza virus, membrane fusion is regulated by the conformational state of the hemagglutinin (ha) protein, which switches from a native (nonfusogenic) structure to a fusion-active (fusogenic) conformation when exposed to the acidic environment of the cellular endosome. the native structure of ha is trapped in a metastable state and that the fusogenic conformation is released by destabilization of native structure2.
references
1. e. wagner, c. plank et al, influenza virus hemagglutinin ha-2 n-terminal fusogenic peptides augment gene transfer by transferrin-polylysine-dna complexes: toward a synthetic virus-like gene-transfer vehicle. proc. nati. acad. sci. usa vol. 89, pp. 7934-7938, september 1992 2. c. m. carr, c. chaudhry, p. s. kim et al. influenza hemagglutinin is spring-loaded by a metastable native conformation. proc. natl. acad. sci. usa vol. 94, pp. 14306–14313
Check Digit Verification of cas no
The CAS Registry Mumber 92000-76-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,2,0,0 and 0 respectively; the second part has 2 digits, 7 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 92000-76:
(7*9)+(6*2)+(5*0)+(4*0)+(3*0)+(2*7)+(1*6)=95
95 % 10 = 5
So 92000-76-5 is a valid CAS Registry Number.
92000-76-5Relevant articles and documents
Modified epimorphin
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, (2008/06/13)
Disclosed herein are a modified epimorphin obtained by adding a hydrophilic peptide composed of 5 to 99 amino acids to at least one terminus of a polypeptide containing the functional domain of epimorphin, and a modified epimorphin composed of a polypeptide having a structure wherein a hydrophobic domain adjacent to the C-terminus of the whole-length epimorphin consisting of a coiled coil domain (1) on the N-terminal side, a functional domain (2) at the center, a coiled coil domain (3) on the C-terminal side and the hydrophobic domain (4) adjacent to the C-terminus has been deleted from the whole-length epimorphin, and at least part of amino acids have been deleted from the terminal side of at least one of the coiled coil domains (1) and (3) as well. The invention also discloses a variant modified epimorphin obtained by making partial substitution, deletion and/or insertion of amino acids in the amino acid sequence of the modified epimorphin, wherein the variant maintains the function of the original sequence. The invention further discloses DNAs encoding the modified epimorphin and variant thereof, recombinant vectors containing the DNAs, transformants obtained by introducing the recombinant vectors, and a production method of the modified epimorphin and the variants thereof making use of the transformant.
