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Your Position: > Antibody > Fusion glycoprotein F0 > RSF-MY2092

Monoclonal Anti-Mumps virus Fusion glycoprotein F0 Antibody, Human IgG1 (5A3) (MALS verified)

  • Source

    Monoclonal Anti-Mumps virus Fusion glycoprotein F0 Antibody, Human IgG1 (5A3) is a chimeric monoclonal antibody recombinantly expressed from HEK293, which combines the variable region of a mouse monoclonal antibody with Human constant domain.

  • Clone

    5A3

  • Species

    Mouse

  • Isotype

    Human IgG1 | Human Kappa

  • Conjugate

    Unconjugated

  • Antibody Type

    Recombinant Monoclonal

  • Reactivity

    Virus

  • Immunogen

    Recombinant Mumps virus (strain Miyahara vaccine) (MuV) Fusion glycoprotein F0 is expressed from human 293 cells.

  • Specificity

    Specifically recognizes Mumps virus (strain Miyahara vaccine) (MuV) Fusion glycoprotein F0.

  • Application
    ApplicationRecommended Usage
    Western Blot10-0.02 ug/mL
    ELISA0.1-31 ng/mL
  • Purity

    >95% as determined by SDS-PAGE.

    >90% as determined by SEC-MALS.

  • Purification

    Protein A purified/ Protein G purified

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Fusion glycoprotein F0 SDS-PAGE

Monoclonal Anti-Mumps virus Fusion glycoprotein F0 Antibody, Human IgG1 (5A3) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS
Fusion glycoprotein F0 MALS images

The purity of Monoclonal Anti-Mumps virus Fusion glycoprotein F0 Antibody, Human IgG1 (5A3) (Cat. No. RSF-MY2092) is more than 90% and the molecular weight of this protein is around 135-160 kDa verified by SEC-MALS.

Bioactivity-ELISA
 Fusion glycoprotein F0 ELISA

Immobilized Mumps virus (strain Miyahara vaccine) (MuV) Fusion glycoprotein F0, His Tag (Cat. No. RSF-V52H4) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Mumps virus Fusion glycoprotein F0 Antibody, Human IgG1 (5A3) (Cat. No. RSF-MY2092) with a linear range of 0.1-4 ng/mL (QC tested).

Western Blot
 Fusion glycoprotein F0 WESTERN BLOT

Detection of Monoclonal Anti-Mumps virus Fusion glycoprotein F0 antibody-5A3, Human IgG1 | Human Kappa ,HEK by Western Blot. Monoclonal Anti-Mumps virus Fusion glycoprotein F0 antibody-5A3, Human IgG1 | Human Kappa,HEK at 0.02ug/ml dilution + Mumps virus (strain Miyahara vaccine) (MuV) Fusion glycoprotein F0, His Tag (MALS verified), His Tag at 400ng.

Secondary Antibody: (HFC)-HRP Goat Anti-Human IgG,Fcγ fragment specific (min X Bov,Hrs,Ms Sr Prot) at 1/2000 dilution.

Predicted band size: 53-75 kDa 12% Bis-Tris Protein Gel.

  • Background
    The two surface glycoproteins of the mumps virus are the hemagglutinin-neuraminidase (HN) and Fusion proteins. These glycoproteins are essential for viral entry to host cells, and the spread of newly formed virions. The mumps fusion protein (F) is a 538-amino acid, class one fusion surface glycoprotein. It is responsible for the membrane fusion of virus and host cell. The un-cleaved protein has three hydrophobic regions: an amino-terminal signal peptide, an amino terminal region of F1 and the carboxyl-terminal membrane domain. This protein starts as a precursor molecule (F0), and is then cleaved into the active protein by the recognition of a R-X-L/R-R motif by a host endoprotease (furin). The F protein contains two disulfide-linked polypeptides (F1 and F2).
  • Clinical and Translational Updates

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