Influenza A virus (H5N1/HA1) Antibody [L10F5]

Catalog No.: F3732

Application: Reactivity: Influenza A

Lane 1: H5N1 recombinant protein

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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
WB1:3000

Application
WB, ELISA

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

Predicted MW
64 kDa

Datasheet & SDS

生物学的記述

Specificity
Influenza A virus (H5N1/HA1) Antibody [L10F5] detects exogenous levels of total Influenza A virus (H5N1/HA1) protein.

Clone
L10F5

Synonym(s)
Hemagglutinin; HA

Background
Influenza A virus (H5N1/HA1) is the receptor-binding N-terminal subunit of hemagglutinin (HA), a class I viral fusion glycoprotein synthesized as HA0 precursor and cleaved by host furin at multibasic sites (characteristic of highly pathogenic H5N1) into disulfide-linked HA1 (residues ~1-328) and HA2 (~221 aa). HA1 forms a membrane-distal globular head domain atop the HA2 stalk, composed of antiparallel β-sheets with mixed α/β motifs, featuring the sialic acid receptor-binding site (RBS, key residues Gln226, Gly228 for α2,3-linkage preference), 130-loop/220-loop/190-helix defining antigenic sites, and N-linked glycans (~7 sites) modulating immunogenicity and stability. Trimeric HA1 mediates attachment to sialylated glycans on host respiratory epithelia, triggering receptor-mediated endocytosis; endosomal acidification (pH 5.0-5.5) induces irreversible HA1 dissociation from HA2, exposing HA2 fusion peptide for viral-endosomal membrane fusion and vRNP release into cytoplasm. H5N1 HA1's enhanced acid stability and multibasic cleavage enable systemic replication, high virulence (60% human CFR), and zoonotic potential via receptor-binding adaptations (e.g., Q226L).

Background

Influenza A virus (H5N1/HA1) is the receptor-binding N-terminal subunit of hemagglutinin (HA), a class I viral fusion glycoprotein synthesized as HA0 precursor and cleaved by host furin at multibasic sites (characteristic of highly pathogenic H5N1) into disulfide-linked HA1 (residues ~1-328) and HA2 (~221 aa). HA1 forms a membrane-distal globular head domain atop the HA2 stalk, composed of antiparallel β-sheets with mixed α/β motifs, featuring the sialic acid receptor-binding site (RBS, key residues Gln226, Gly228 for α2,3-linkage preference), 130-loop/220-loop/190-helix defining antigenic sites, and N-linked glycans (~7 sites) modulating immunogenicity and stability. Trimeric HA1 mediates attachment to sialylated glycans on host respiratory epithelia, triggering receptor-mediated endocytosis; endosomal acidification (pH 5.0-5.5) induces irreversible HA1 dissociation from HA2, exposing HA2 fusion peptide for viral-endosomal membrane fusion and vRNP release into cytoplasm. H5N1 HA1's enhanced acid stability and multibasic cleavage enable systemic replication, high virulence (60% human CFR), and zoonotic potential via receptor-binding adaptations (e.g., Q226L).

References
[1] Sriwilaijaroen N, et al. Proc Jpn Acad Ser B Phys Biol Sci. 2012;88(6):226-49. [2] Lazniewski M, et al. Brief Funct Genomics. 2018 Nov 26;17(6):415-427.

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%