JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB74560

Recombinant Mumps virus wild-type, Gloucester strain, nucleocapsid protein

Be the first to review this product! Submit a review

|

(3 Publications)

Recombinant Mumps virus wild-type, Gloucester strain, nucleocapsid protein is a Mumps virus Miyahara vaccine Full Length protein, expressed in Saccharomyces cerevisiae , with >95%, suitable for ELISA, WB, SDS-PAGE.

View Alternative Names

NP, N, Nucleoprotein, Nucleocapsid protein, Protein N, NP, Nucleoprotein

1 Images
SDS-PAGE - Recombinant Mumps virus wild-type, Gloucester strain, nucleocapsid protein (AB74560)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Mumps virus wild-type, Gloucester strain, nucleocapsid protein (AB74560)

SDS-PAGE showing ab74560 at approximately 66kDa. (1.2 μg/lane).

Key facts

Purity

>95% SDS-PAGE

Expression system

Saccharomyces cerevisiae

Tags

Tag free

Applications

ELISA, SDS-PAGE, WB

applications

Biologically active

No

Accession

P21186

Animal free

No

Carrier free

No

Species

Mumps virus Miyahara vaccine

Reconstitution

Reconstitute in water, 50% glycerol

Storage buffer

Constituents: PBS

storage-buffer

style
left-column

Complementary Products

Proteins & Peptides

AB273530

Recombinant Human coronavirus SARS-CoV-2 nucleocapsid protein (His tag)

ELISA - Recombinant Human coronavirus SARS-CoV-2 nucleocapsid protein (His tag) (AB273530)

  • 0
  • 0
Proteins & Peptides

AB269104

Recombinant human HIP2/LIG protein (Active)

Functional Studies - Recombinant human HIP2/LIG protein (Active) (AB269104)

  • 0
  • 0
Proteins & Peptides

AB274662

Native Parainfluenza Virus type 3 protein

  • 0
  • 0
Proteins & Peptides

AB274661

Native Parainfluenza Virus type 2 protein

  • 0
  • 0
style
left-column

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"5 µg/mL", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1 µg/mL", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1.2 µg/mL", "notes":"<p></p>" } } }
style
left-column
style
left-column

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":null,"tags":[]}]
style
left-column

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle|Reconstitute for long term storage
False
style
left-column

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Mumps virus wild-type Gloucester strain nucleocapsid protein plays an important role in the encapsidation of the viral RNA genome which facilitates the replication process of the virus. This protein also known as NP has a mass of approximately 57 kDa and expresses itself in infected host cells where it forms a nucleocapsid structure. The nucleocapsid protein interacts tightly with viral RNA protecting it from host nucleases and serving as a template for viral RNA synthesis.
Biological function summary

The nucleocapsid protein of the Mumps virus Gloucester strain functions as a primary structural component of the virus. It is not a part of a multi-protein complex outside of its encapsulation role although it forms oligomeric structures important for its function. By interacting with other viral proteins like phosphoprotein (P) and large protein (L) it facilitates the localization and assembly of viral components which is essential for virus replication and transcription processes.

Pathways

This nucleocapsid protein interacts directly with the virus replication and transcription machinery. It is situated within the Mumps virus life cycle pathway where it drives the replication of viral RNA. The nucleocapsid protein closely associates with the P and L proteins in these pathways enabling efficient synthesis of new viral genomes and the production of viral mRNA required for the assembly of new virions.

The nucleocapsid protein of the Mumps virus Gloucester strain is central to the pathology of mumps disease. The spread and replication of the virus within the host cells lead to systemic infections characterized by swelling of the salivary glands. There is also a risk of complications such as meningitis and encephalitis. The nucleocapsid protein's interaction with the viral P protein remains key to understanding its role in mumps-related pathogenesis.
style
left-column

Specifications

Form

Lyophilized

Additional notes

ab74560 is purified by ultracentifugation.

style
left-column

General info

Function

Forms the helical nucleocapsid (NC) with 12.71 N subunits per helical turn and a rise of 5.3 Angstrom per N subunit, protecting the genome from nucleases (By similarity). The encapsidated genomic RNA serves as template for transcription and replication; encapsidation by N is coupled to RNA synthesis (By similarity). Forms the encapsidation complex with the phosphoprotein protein P (By similarity). Before encapsidation, the newly synthesized free N protein, so-called N0, is chaperoned by P (By similarity).

Sequence similarities

Belongs to the paramyxoviruses nucleocapsid family.

style
left-column

Product protocols

style
left-column

Target data

Forms the helical nucleocapsid (NC) with 12.71 N subunits per helical turn and a rise of 5.3 Angstrom per N subunit, protecting the genome from nucleases (By similarity). The encapsidated genomic RNA serves as template for transcription and replication; encapsidation by N is coupled to RNA synthesis (By similarity). Forms the encapsidation complex with the phosphoprotein protein P (By similarity). Before encapsidation, the newly synthesized free N protein, so-called N0, is chaperoned by P (By similarity).
See full target information N
style
left-column

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Vaccines 8: PubMed32325874

2020

Protective Malaria Vaccine in Mice Based on the Circumsporozoite Protein Fused with the Mumps Nucleocapsid Protein.

Applications

Unspecified application

Species

Unspecified reactive species

Rodolfo F Marques,Alba Marina Gimenez,Eduardo Aliprandini,Janaina T Novais,Diego P Cury,Ii-Sei Watanabe,Mariana R Dominguez,Eduardo L V Silveira,Rogerio Amino,Irene S Soares

Epidemiology and infection 148:e17 PubMed32014073

2020

Application of a fast and cost-effective 'three-in-one' MMR ELISA as a tool for surveying anti-MMR humoral immunity: the Hungarian experience.

Applications

Unspecified application

Species

Unspecified reactive species

K Böröcz,Z Csizmadia,Á Markovics,N Farkas,J Najbauer,T Berki,P Németh

IEEE journal of solid-state circuits 53:2054-2064 PubMed30559530

2018

High-Density Redox Amplified Coulostatic Discharge-Based Biosensor Array.

Applications

Unspecified application

Species

Unspecified reactive species

Alexander C Sun,Enrique Alvarez-Fontecilla,A G Venkatesh,Eliah Aronoff-Spencer,Drew A Hall
View all publications
style
left-column
style
left-column
style
right-column

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com