SAB3500092

Sigma-Aldrich

Anti-Seasonal H1N1 Nucleocapsid Protein antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):
Anti-NP, Anti-Common flu NP
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

viral

application(s)

indirect ELISA: suitable

conjugate

unconjugated

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

General description

Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus (S-OIV) was identified in specimens obtained from patients in Mexico and the United States. The influenza A virus polymerase transcribes and replicates eight virion RNA (vRNA) segments. The nucleocapsid protein (NP) is produced among these segments. It is thought to control whether mRNA or cRNA is produced. NP has multiple functions during the virus life cycle. It possesses regions that are highly conserved among influenza A, B and C viruses. It is studied that NP mutations affected the efficient incorporation of multiple viral-RNA (vRNA) segments into progeny virions. This indicates that the conserved amino acids in NP might be critical for the assembly and incorporation of sets of eight vRNA segments. This antibody is specific for the seasonal H1N1 influenza NP and will not recognize the corresponding NP sequence from the swine-origin H1N1 influenza (A/California/14/2009 (H1N1)).

Immunogen

NP antibody was raised against a synthetic peptide from the Seasonal H1N1 NP protein.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Target description

Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus (S-OIV) was identified in specimens obtained from patients in Mexico and the United States. The influenza A virus polymerase transcribes and replicates eight virion RNA (vRNA) segments, among which the nucleocapsid protein (NP), thought to control whether mRNA or cRNA is produced. The nucleoprotein (NP), which has multiple functions during the virus life cycle, possesses regions that are highly conserved among influenza A, B, and C viruses. It was recently found several NP mutations that affected the efficient incorporation of multiple viral-RNA (vRNA) segments into progeny virions even though a single vRNA segment was incorporated efficiently. This indicates that the respective conserved amino acids in NP may be critical for the assembly and/or incorporation of sets of eight vRNA segments. This antibody is specific for the seasonal H1N1 influenza NP and will not recognize the corresponding NP sequence from the swine-origin H1N1 influenza (A/California/14/2009 (H1N1)).

Linkage

The action of this antibody can be blocked using blocking peptide SBP3500092.

Physical form

Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Mutational analysis of conserved amino acids in the influenza A virus nucleoprotein.
Li Z, et al.
Journal of Virology, 83(9), 4153-4162 (2009)
Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication.
Newcomb L L, et al.
Journal of Virology, 83(1), 29-36 (2009)

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