Influenza A Virus M2 Protein Antibody [L21L24]

Catalog No.: F2238

Application: Reactivity: Influenza A

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
IF1:2000

Application
IF

Source
Mouse Monoclonal Antibody

Reactivity
Influenza A

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Datasheet & SDS

生物学的記述

Specificity
Influenza A Virus M2 Protein Antibody [L21L24] detects exogenous levels of total Influenza A Virus M2 protein.

Clone
L21L24

Synonym(s)
Influenza A virus matrix protein M2; Matrix protein 2; Membrane ion channel M2; Membrane protein M2; Proton channel protein M2

Background
The Influenza A Virus (IAV) M2 protein is a 97-amino acid, integral membrane viroporin essential for the viral life cycle, functioning as a homotetrameric, pH-activated, proton-selective ion channel. Its structure consists of an N-terminal ectodomain (residues 1–24) critical for virion incorporation, a transmembrane domain (residues 25–43) forming the channel core, and a C-terminal domain (residues 44–97) that includes an amphipathic helix and an unstructured tail involved in virus assembly and budding. Key residues, His37 and Trp41, serve as the proton sensor and channel gate, respectively. Upon endosomal acidification during viral entry, M2 mediates proton influx into the virion, facilitating release of viral ribonucleoproteins for replication. Subsequently, M2 maintains optimal pH in the trans-Golgi network to prevent premature hemagglutinin activation, while its C-terminal amphipathic helix induces membrane curvature required for viral budding and scission. M2 activity is regulated by pH and host protein interactions, and although it is a target of antivirals like amantadine, drug resistance is common due to mutations in the transmembrane domain.

Background

The Influenza A Virus (IAV) M2 protein is a 97-amino acid, integral membrane viroporin essential for the viral life cycle, functioning as a homotetrameric, pH-activated, proton-selective ion channel. Its structure consists of an N-terminal ectodomain (residues 1–24) critical for virion incorporation, a transmembrane domain (residues 25–43) forming the channel core, and a C-terminal domain (residues 44–97) that includes an amphipathic helix and an unstructured tail involved in virus assembly and budding. Key residues, His37 and Trp41, serve as the proton sensor and channel gate, respectively. Upon endosomal acidification during viral entry, M2 mediates proton influx into the virion, facilitating release of viral ribonucleoproteins for replication. Subsequently, M2 maintains optimal pH in the trans-Golgi network to prevent premature hemagglutinin activation, while its C-terminal amphipathic helix induces membrane curvature required for viral budding and scission. M2 activity is regulated by pH and host protein interactions, and although it is a target of antivirals like amantadine, drug resistance is common due to mutations in the transmembrane domain.

References
[1] Cady SD, et al. Biochemistry. 2009 Aug 11;48(31):7356-64. [2] Ma C, et al. Proc Natl Acad Sci U S A. 2009 Jul 28;106(30):12283-8.

PVDFメンブレン孔径参考表

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%