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MAB10207

Sigma-Aldrich

Anti-Fusion Glycoprotein of Human parainfluenzavirus Type 3 Antibody, clone 9-4-3

ascites fluid, clone 9-4-3, Chemicon®

Synonym(s):
PI3
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

ascites fluid

antibody product type

primary antibodies

clone

9-4-3, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

immunofluorescence: suitable

isotype

IgG1

UniProt accession no.

shipped in

wet ice

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antibody form

ascites fluid

antibody form

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antibody form

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antibody form

ascites fluid

clone

9-4-3, monoclonal

clone

1H10-6, monoclonal

clone

450-11G-8A-5E, monoclonal

clone

monoclonal

species reactivity

human

species reactivity

human

species reactivity

human

species reactivity

human

manufacturer/tradename

Chemicon®

manufacturer/tradename

Chemicon®

manufacturer/tradename

Chemicon®

manufacturer/tradename

Chemicon®

technique(s)

immunofluorescence: suitable

technique(s)

immunofluorescence: suitable, inhibition assay: suitable (hemagglutination)

technique(s)

immunofluorescence: suitable

technique(s)

immunofluorescence: suitable

General description

Human parainfluenza virus type 3 (PI3 virus) causes mild to severe respiratory tract infection in infants. PI3 virus is an enveloped RNA virus and possesses two glycoproteins, hemagglutinin-neuraminidase (HN) and fusion (F), at its external surface. These two glycoproteins are known to be responsible for initiation and progress of the infection process

Immunogen

Fusion (F) glycoprotein of human parainfluenzavirus type 3

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Antiviral effects of glycosylation and glucose trimming inhibitors on human parainfluenza virus type 3
Tanaka, Yoshikazu, et al
Antiviral research, 72, 1-9 (2006)
M A Horga et al.
Journal of virology, 74(24), 11792-11799 (2000-11-23)
Viral interference is characterized by the resistance of infected cells to infection by a challenge virus. Mechanisms of viral interference have not been characterized for human parainfluenza virus type 3 (HPF3), and the possible role of the neuraminidase (receptor-destroying) enzyme
Laura M Palermo et al.
Journal of virology, 83(13), 6900-6908 (2009-04-24)
Three discrete activities of the paramyxovirus hemagglutinin-neuraminidase (HN) protein, receptor binding, receptor cleaving (neuraminidase), and triggering of the fusion protein, each affect the promotion of viral fusion and entry. For human parainfluenza virus type 3 (HPIV3), the effects of specific
Ying Liu et al.
Virus genes, 56(1), 37-48 (2019-11-27)
Human parainfluenza virus type 3 (HPIV3) causes the majority of childhood viral pneumonia around the world. Fusing the viral and target cell membranes is crucial for its entry into target cells, and the fusion process requires the concerted actions of
Wenyan Xie et al.
PloS one, 10(8), e0136474-e0136474 (2015-08-26)
Human parainfluenza virus type 3 (HPIV3) can cause severe respiratory tract diseases in infants and young children, but no licensed vaccines or antiviral agents are currently available for treatment. Fusing the viral and target cell membranes is a prerequisite for

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