RVFV Gn
Anti-RVFV Gn Recombinant Antibody Products
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- Species Reactivity: RVFV
- Type: Rabbit IgG
- Application: ELISA, Neut, FuncS
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- Species Reactivity: RVFV
- Type: Human IgG
- Application: ELISA, FC, Neut
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- Species Reactivity: RVFV
- Type: Human IgG
- Application: ELISA, FC, Neut
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- Species Reactivity: RVFV
- Type: Human IgG
- Application: ELISA, FC, Neut
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Compare
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- Species Reactivity: RVFV
- Type: Rabbit IgG
- Application: ELISA
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- Species Reactivity: RVFV
- Type: Rabbit IgG
- Application: ELISA
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Compare
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Compare
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Compare
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- Species Reactivity: RVFV
- Type: Human IgG
- Application: ELISA, FC, Neut
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- Species Reactivity: RVFV
- Type: Human scFv
- Application: ELISA, FC, Neut
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- Species Reactivity: RVFV
- Type: Human scFv
- Application: ELISA, FC, Neut
Compare
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- Species Reactivity: RVFV
- Type: Human scFv
- Application: ELISA, FC, Neut
Compare
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- Species Reactivity: RVFV
- Type: Human scFv
- Application: ELISA, FC, Neut
Compare
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- Species Reactivity: RVFV
- Type: Human Fab
- Application: ELISA, FC, Neut
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- Species Reactivity: RVFV
- Type: Human Fab
- Application: ELISA, FC, Neut
Compare
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- Species Reactivity: RVFV
- Type: Human Fab
- Application: ELISA, FC, Neut
Compare
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- Species Reactivity: RVFV
- Type: Human Fab
- Application: ELISA, FC, Neut
Compare
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- Species Reactivity: RVFV
- Type: Rabbit scFv
- Application: ELISA, Neut, FuncS
Compare
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- Species Reactivity: RVFV
- Type: Rabbit Fab
- Application: ELISA, Neut, FuncS
Compare
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For Research Use Only. Not For Clinical Use.
Rift Valley fever virus (RVFV) is an arbovirus endemic to Africa and the Arabian peninsula that causes recurrent epidemics and epizootics. RVFV is of both agricultural and biomedical importance, as infection of livestock results in high incidences of neonatal mortality and zoonosis; human disease ranges from mild self-limiting febrile illness to severe disease characterized by hemorrhagic diatheses, encephalitis, and ocular pathologies. Like all known phleboviruses, RVFV is enveloped and contains a single-stranded, negative- or ambi-sense RNA genome that is divided into three segments: S, M, and L. The M segment encodes the glycoprotein precursor, which is processed into two membrane-anchored glycoproteins, Gn and Gc. The multi-domain phleboviral Gn is structurally distinct and exhibits partial secondary structure similarity with the Gn of hantaviruses and the E1 of alphaviruses.