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Influenza A Matrix Protein antibody | GA2B

Mouse anti Influenza A Matrix Protein

Product Type
Monoclonal Antibody
Clone
GA2B
Isotype
IgG1
Specificity
Influenza A Matrix Protein

Product Code Applications Pack Size List Price Your Price Qty
MCA401
Datasheet Datasheet Datasheet
SDS Safety Datasheet SDS
IF P WB 1 mg loader
List Price Your Price
loader

Mouse anti Influenza A matrix protein 1 antibody, clone GA2B recognizes an epitope within the influenza A matrix protein 1. In both strains of virus used as immunogen to isolate clone GA2B, the matrix protein 1 is a 252 amino acid, highly conserved viral protein playing a crucial role in replication.

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
Viral
Product Form
Purified IgG - liquid
Preparation
Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant.
Buffer Solution
Phosphate buffered saline
Preservative Stabilisers
<0.1% Sodium Azide (NaN3)
Immunogen
Influenza A / Puerto Rico / 8 / 34 (H1N1) and A/Bangkok / 1 / 79 (H3N2) viruses.
Purity
>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.
Regulatory
For research purposes only
Guarantee
12 months from date of despatch

This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.

Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
Immunofluorescence 1/100
Immunohistology - Paraffin
Western Blotting
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls.

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References for Influenza A Matrix Protein antibody

  1. 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.
  2. 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.
  3. Yamamoto, Y. et al. (2008) Avian influenza virus (H5N1) replication in feathers of domestic waterfowl.
    Emerg Infect Dis. 14: 149-51.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. View The Latest Product References
  10. 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.
  11. Kang, S.M. et al. (2009) Induction of long-term protective immune responses by influenza H5N1 virus-like particles.
    PLoS One. 4: e4667.
  12. 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.
  13. Schmolke, M. et al. (2009) Essential impact of NF-kappaB signaling on the H5N1 influenza A virus-induced transcriptome.
    J Immunol. 183: 5180-9.
  14. 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.
  15. 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.
  16. 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.
  17. Moncorgé, O. et al. (2013) Investigation of influenza virus polymerase activity in pig cells.
    J Virol. 87 (1): 384-94.
  18. Khaperskyy, D.A. et al. (2012) Influenza A virus inhibits cytoplasmic stress granule formation.
    FASEB J. 26: 1629-39.
  19. 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.
  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.
  21. 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. 16 (5): 728-42.
  22. 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.
  23. 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.
  24. 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.
  25. Yang, C.H. et al. (2017) Influenza A virus upregulates PRPF8 gene expression to increase virus production.
    Arch Virol. 162 (5): 1223-35.
  26. 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.
  27. Usui, T. et al. (2020) Outbreaks of highly pathogenic avian influenza in zoo birds caused by HA clade 2.3.4.4 H5N6 subtype viruses in Japan in winter 2016.
    Transbound Emerg Dis. 67 (2): 686-697.
  28. Frensing, T. et al. (2016) Influenza virus intracellular replication dynamics, release kinetics, and particle morphology during propagation in MDCK cells.
    Appl Microbiol Biotechnol. 100 (16): 7181-92.
  29. Melano, I. et al. (2021) Effects of Basic Amino Acids and Their Derivatives on SARS-CoV-2 and Influenza-A Virus Infection.
    Viruses. 13 (7):1301.
  30. Soda, K. et al. (2022) Susceptibility of herons (family: Ardeidae) to clade 2.3.2.1 H5N1 subtype high pathogenicity avian influenza virus.
    Avian Pathol. 51 (2): 146-53.
  31. Soda, K. et al. (2022) Susceptibility of common family Anatidae bird species to clade 2.3.4.4e H5N6 high pathogenicity avian influenza virus: an experimental infection study.
    BMC Vet Res. 18 (1): 127.
  32. Kwasnik, M. et al. (2023) Protein-Coding Region Derived Small RNA in Exosomes from Influenza A Virus-Infected Cells.
    Int J Mol Sci. 24(1):867.
  33. Yang, M.L. et al. (2023) Upregulation of galectin-3 in influenza A virus infection promotes viral RNA synthesis through its association with viral PA protein.
    J Biomed Sci. 30 (1): 14.
  34. Soda, K. et al. (2023) Susceptibility of common dabbling and diving duck species to clade 2.3.2.1 H5N1 high pathogenicity avian influenza virus: an experimental infection study.
    J Vet Med Sci. 85 (9): 942-9.
  35. Kühnl, A. et al. (2018) Late Endosomal/Lysosomal Cholesterol Accumulation Is a Host Cell-Protective Mechanism Inhibiting Endosomal Escape of Influenza A Virus.
    mBio. 9 (4): e01345-18.

Immunofluorescence

Immunohistology - Paraffin

Western Blotting

RRID
AB_322157
UniProt
P03485
P03487
Entrez Gene
M1
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

MCA401

150420 158367 165701

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