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Puumala Virus Nucleocapsid Antibody | 7693

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SKU:
223-7693-GEN
NULL341.00 - NULL647.00

Description

Puumala Virus Nucleocapsid Antibody | 7693 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Virus

Homology: N/A

Immunogen: Puumala virus nucleocapsid antibody was raised against a 19 amino acid peptide near the amino terminus of the Puumala virus nucleocapsid.
The immunogen is located within amino acids 130 - 180 of Puumala Virus Nucleocapsid.

Research Area: Infectious Disease

Tested Application: E

Application: Puumala virus nucleocapsid antibody can detect 10ng Puumala virus nucleocapsid peptide in ELISA at 1 μg/ml.

Specificiy: N/A

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: N/A

Validation: N/A

Isoform: N/A

Purification: Puumala virus nucelocapsid antibody is affinity chromatography purified via peptide column.

Clonality: Polyclonal

Clone: N/A

Isotype: IgG

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Puumala virus nucleocapsid antibody is supplied in PBS containing 0.02% sodium azide.

Concentration: 1 mg/mL

Storage Condition: Puumala virus nucleocapsid antibody can be stored at 4˚C for three months and -20˚C, stable for up to one year.

Alternate Name: Puumala Virus Nucleocapsid Antibody: Nucleoprotein, Nucleocapsid protein, Protein N

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: Puumala virus (PUUV) is a rodent-borne hantavirus of the family Bunyaviridae, an enveloped, negative-sense RNA viruses with a tripartite genome that can cause hantavirus pulmonary syndrome (HPS) and is highly homologous to the protype hantavirus Hantaan virus (1) . Like other hantaviruses, the PUUV glycoprotein is synthesized as a precursor that is posttranslationally processed into two glycoproteins G1 (Gn) and G2 (Gc) . These glycoproteins interact with the PUUV nucleocapsid (NP) protein through their cytoplasmic tail, and this association has been suggested to be crucial to the binding of the ribonucleoprotein of the PUUV and the assembly of the virus particle (2) .

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