Influenza A Matrix Protein antibody | GA2B
Mouse anti Influenza A matrix protein 1 antibody, clone GA2B can be used in influenza A IFA typing in conjunction with Mouse anti Influenza A matrix protein, clone AA5H.
- Target Species
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant.
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide
- Influenza A / Puerto Rico / 8 / 34 (H1N1) and A/Bangkok / 1 / 79 (H3N2) viruses.
- >90% IgG content as established by SDS PAGE
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from immunised BALB/c mice were fused with cells of the P3 Ag8.653 mouse myeloma cell line.
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
- 12 months from date of despatch
- Entrez Gene
- GO Terms
- GO:0005886 plasma membrane
- GO:0003723 RNA binding
- GO:0005829 cytosol
- GO:0005198 structural molecule activity
- GO:0005654 nucleoplasm
- GO:0019064 viral envelope fusion with host membrane
- GO:0019061 uncoating of virus
- GO:0019065 receptor-mediated endocytosis of virus by host
- GO:0019070 viral genome maturation
- GO:0019072 viral genome packaging
- GO:0019076 release of virus from host
- GO:0019083 viral transcription
- GO:0030666 endocytic vesicle membrane
- GO:0030683 evasion by virus of host immune response
- GO:0031904 endosome lumen
- GO:0042025 host cell nucleus
- GO:0046796 viral genome transport in host cell
- GO:0055036 virion membrane
- GO:0016020 membrane
- For research purposes only
Applications of Influenza A Matrix Protein antibody
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Paraffin|
Secondary Antibodies Available
Product Specific References
References for Influenza A Matrix Protein antibody
Latham, T. & Galarza, J.M. (2001) Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins.
J Virol. 75 (13): 6154-65.
Zhirnov, O.P. & Klenk, H.D. (1997) Histones as a target for influenza virus matrix protein M1.
Virology. 235 (2): 302-10.
Viemann, D. et al. (2011) H5N1 virus activates signaling pathways in human endothelial cells resulting in a specific imbalanced inflammatory response.
J Immunol. 186 (1): 164-73.
Yamamoto, Y. et al. (2008) Avian influenza virus (H5N1) replication in feathers of domestic waterfowl.
Emerg Infect Dis. 14: 149-51.
Doucet, J.D. et al. (2011) Endogenously expressed matrix protein M1 and nucleoprotein of influenza A are efficiently presented by class I and class II major histocompatibility complexes.
J Gen Virol. 92 (Pt 5): 1162-71.
Tanimura N et al. (2006) 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.
Kirkeby, S. et al. (2009) 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.
Pauli, E.K. et al. (2008) Influenza A virus inhibits type I IFN signaling via NF-kappaB-dependent induction of SOCS-3 expression.
PLoS Pathog. 4(11): e1000196.
Eierhoff, T. et al. (2010) The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells.
PLoS Pathog. 6. pii: e1001099.
Wang, D. et al. (2010) 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.
Kang, S.M. et al. (2009) Induction of long-term protective immune responses by influenza H5N1 virus-like particles.
PLoS One. 4: e4667.
Luig, C. et al. (2010) 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.
Schmolke, M. et al. (2009) Essential impact of NF-kappaB signaling on the H5N1 influenza A virus-induced transcriptome.
J Immunol. 183: 5180-9.
Reinhardt, J. and Wolff, T. (2000) 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.
Das, S.C. et al. (2012) 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.
Liu, Y.V. et al. (2011) 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.
Moncorgé, O. et al. (2013) Investigation of influenza virus polymerase activity in pig cells.
J Virol. 87 (1): 384-94.
Khaperskyy, D.A. et al. (2012) Influenza A virus inhibits cytoplasmic stress granule formation.
FASEB J. 26: 1629-39.
Friesenhagen, J. et al. (2012) Highly pathogenic avian influenza viruses inhibit effective immune responses of human blood-derived macrophages.
J Leukoc Biol. 92: 11-20.
Londrigan, S.L. et al. (2015) Infection of Mouse Macrophages by Seasonal Influenza Viruses Can Be Restricted at the Level of Virus Entry and at a Late Stage in the Virus Life Cycle.
J Virol. 89 (24): 12319-29.
Sadewasser, A. et al. (2017) Quantitative proteomic approach identifies Vpr binding protein as novel host factor supporting influenza A virus infections in human cells.
Mol Cell Proteomics. Mar 13. pii: mcp.M116.065904. doi: 10.1074/mcp.M116.065904. [Epub ahead of print]
Liu, Y.V. et al. (2015) Recombinant virus-like particles elicit protective immunity against avian influenza A(H7N9) virus infection in ferrets.
Vaccine. 33 (18): 2152-8.
Herrmann, V.L. et al. (2015) Cytotoxic T cell vaccination with PLGA microspheres interferes with influenza A virus replication in the lung and suppresses the infectious disease.
J Control Release. 216: 121-31.
Huang, M.T. et al. (2015) DcR3 suppresses influenza virus-induced macrophage activation and attenuates pulmonary inflammation and lethality.
J Mol Med (Berl). 93 (10): 1131-43.
Al-Mubarak, F. et al. (2015) Identification of morphological differences between avian influenza A viruses grown in chicken and duck cells.
Virus Res. 199: 9-19.
Yang, C.H. et al. (2017) Influenza A virus upregulates PRPF8 gene expression to increase virus production.
Arch Virol. 162 (5): 1223-35.
Smith, G.E. et al. (2017) Neuraminidase-based recombinant virus-like particles protect against lethal avian influenza A(H5N1) virus infection in ferrets.
Virology. 509: 90-97.