Influenza A H1N1/H3N2 M1 Antibody (GA2B) - (A/Puerto Rico/8/1934), (A/Bangkok/1/1979) - BSA Free

• Reactivity: V-Vi
• Applications: WB, IHC
• Clone: GA2B
• Clonality: Monoclonal
• Host: Mouse
• Conjugate: Unconjugated
• Format: BSA Free
• Concentration: 1.0 mg/ml

Influenza A H1N1/H3N2 M1 Antibody (GA2B) - (A/Puerto Rico/8/1934), (A/Bangkok/1/1979) - BSA Free Summary

• Immunogen: Influenza A / Puerto Rico / 8 / 34 (H1N1) and A/Bangkok / 1 / 79 (H3N2) viruses
• Specificity: Influenza A H1N1/H3N2 M1. (A/Puerto Rico/8/1934) (A/Bangkok/1/1979). Recognizes an epitope within the Influenza A matrix protein.
• Isotype: IgG1
• Clonality: Monoclonal
• Host: Mouse
• Purity: Protein A purified

Applications/Dilutions

• Dilutions:
  • Immunohistochemistry 1:10-1:500
  • Immunohistochemistry-Paraffin 1:10-1:500
  • Western Blot 1:100-1:2000

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: PBS
• Preservative: <0.1% Sodium Azide
• Concentration: 1.0 mg/ml
• Purity: Protein A purified

Background

Influenza virus type A matrix protein, also known as M1, is composed of a 252 amino acid sequence and is type-specific in influenza viruses. It is located inside the viral lipid envelope and plays a key role in virus assembly and replication. M1 can be isolated from particles by removing the envelope with detergents and reducing the pH to 4.0. Influenza viruses are a common and widely spread infectious agent. Like many other viruses, influenza virus are constantly undergoing mutations and thereby avoiding the immune system. The Influenza A Virus M proteins form a continuous shell on the inner side of the lipid bilayer, maintaining the structural integrity of the virus particle through hydrophobic interactions.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for Influenza A Virus Antibody (NB100-66552)(16)

Publications using NB100-66552

• Das, SC et al. The Highly Conserved Arginine Residues at Positions 76 through 78 of Influenza A Virus Matrix Protein M1 Play an Important Role in Viral Replication by Affecting the Intracellular Localization of M1. J Virol 86: 1522-30. 2012-01-01 [PMID: 22090133]
• Liu, YV et al. Chimeric severe acute respiratory syndrome coronavirus (SARS-CoV) S glycoprotein and influenza matrix 1 efficiently form virus-like particles (VLPs) that protect mice against challenge with SARS-CoV. Vaccine 29: 6606-13. 2011-01-01 [PMID: 21762752]
• Doucet, JD et al. Endogenously-expressed influenza A M1 and NP proteins are efficiently presented by class-I and -II major histocompatibility complexes. J Gen Virol. 2011-02-09 [PMID: 21307226]
• Viemann, D et al. H5N1 Virus Activates Signaling Pathways in Human Endothelial Cells Resulting in a Specific Imbalanced Inflammatory Response. J Immunol. 2010-11-24 [PMID: 21106851]
• Eierhoff, T et al. The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells. PLoS Pathog. 6. pii: e1001099. 2010-01-01 [PMID: 20844577]
• Luig, C et al. MAP kinase-activated protein kinases 2 and 3 are required for influenza A virus propagation and act via inhibition of PKR. FASEB J 24: 4068-77. 2010-01-01 [PMID: 20484669]
• Wang, D et al. The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles. J Virol 84: 4673-81. 2010-01-01 [PMID: 20181696]
• Schmolke, M et al. Essential impact of NF-kappaB signaling on the H5N1 influenza A virus-induced transcriptome. J Immunol 183: 5180-9. 2009-01-01 [PMID: 19786538]
• Kirkeby, S et al. Infection with human H1N1 influenza virus affects the expression of sialic acids of metaplastic mucous cells in the ferret airways. Virus Res 144: 225-32. 2009-01-01 [PMID: 19447147]
• Kang, SM et al. Induction of long-term protective immune responses by influenza H5N1 virus-like particles. PLoS One 4: e4667. 2009-01-01 [PMID: 19252744]
• Pauli, EK et al. Influenza A virus inhibits type I IFN signaling via NF-kappaB-dependent induction of SOCS-3 expression. PLoS Pathog 4(11): e1000196. 2008-01-01 [PMID: 18989459]
• Yamamoto, Y et al. Avian influenza virus (H5N1) replication in feathers of domestic waterfowl. Emerg Infect Dis 14: 149-51. 2008-01-01 [PMID: 18258095]
• Tanimura, N et al. Pathology of fatal highly pathogenic H5N1 avian influenza virus infection in large-billed crows (Corvus macrorhynchos) during the 2004 outbreak in Japan. Vet Pathol;43(4):500-9. 2006-07-01 [PMID: 16846992]
• Latham, T et al. Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. J Virol75: 6154 - 6165. 2001-01-01 [PMID: 11390617]
• Reinhardt, J Wolff, T. The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. Vet Microbiol 74: 87-100. 2000-01-01 [PMID: 10799781]
• Zhirnov, O et al. Histones as a target for influenza virus matrix protein M1. Virology 235: 302-310. 1997-01-01 [PMID: 9281510]

FAQs for Influenza A Virus Antibody (NB100-66552). (Showing 1 - 1 of 1 FAQs).

1. I am looking for an antibody to be used against the influenza A M1 (matrix) protein of the PR8 strain, both in western blot and immunofluorescence microscopy. Your antibody NB100-66552 appears to be well suited for this. However, I want to use it for mutant proteins that differ in amino acids 97 and 100. Both these amino acids are located on the surface of the intact M1 protein. If the antibody binds near these amino acids, a difference in binding efficiency might occur that could influence my results. Therefore, I was wondering if you know to which part of the M1 protein this antibody binds.
   • The lab has informed me that the epitope has not been mapped. I am very sorry that we do not have any helpful information! (We unfortunately do no epitope map our antibodies. All specific interactions and bindings are determined by experiment and will be listed in the Specificity section on our datasheet. If the specificity you are looking for is not listed, it has not yet been tested. If would like to try any of our antibodies in your experiment utilizing untested applications or species, you would qualify for our Innovators Reward Program.