H1N1 Nucleoprotein流感B核蛋白多株抗體#11675-02,可應用於WBELISA,在WB分析其靈敏度0.5ngELISA偵測靈敏度為0.00975ng。



Influenza A Nucleoprotein / NP Antibody (Antigen Affinity Purified)  


 

H1N1 Nucleoprotein / NP Antibody (Antigen Affinity Purified) Datasheet

Order or Inquire for H1N1 Nucleoprotein / NP Antibody product
Detection limit is 0.5 ng/lane in WB
Detection limit is 0.00975 ng/well in ELISA

 

H1N1 Nucleoprotein / NP Antibody Product Information

Immunogen :

Recombinant H1N1 NP protein (Catalog#11675-V08B)


Antibody Type : Rabbit Polyclonal Antibody ( Antibody Purification Platform )
Ig Type :

Rabbit IgG


Formulation :0.2 μm filtered solution in PBS with 5% trehalose
Preparation :

Produced in rabbits immunized with purified, human cell-derived, recombinant Influenza A virus H1N1 Nucleoprotein / NP, NP specific IgG was purified by H1N1 Nucleoprotein / NP? affinity chromatography.


 

H1N1 Nucleoprotein / NP Antibody Usage Guide

Specificity :


Influenza A H1N1 Nucleoprotein


Western blot :This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect H1N1 NP in WB. Using a DAB detection system, the detection limit for H1N1 NP is approximately 1 ng/lane under non-reducing conditions and 0.5 ng/lane under reducing conditions.
Direct ELISA :This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect H1N1 NP. The detection limit for H1N1 NP is approximately 0.00975 ng/well.
Storage :This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.

 

H1N1 Nucleoprotein / NP Antibody Related Products & Topics

Related Areas:

Proteins:

Antibodies:

 

H1N1 Nucleoprotein / NP Antibody Background

Influenza (flu) is a respiratory infection in mammals and birds. This virus is divided into three main types (A, B and C). Influenza A is found in a wide variety of bird and mammal species. Influenza B is largely confined to humans and is an important cause of morbidity. Influenza C infects humans, dogs and pigs, sometimes causing both severe illness and local epidemics. Influenza A is further divided into subtypes based on differences in the membrane proteins hemagglutinin (HA) and neuraminidase (NA). The notation HhNn is used to refer to the subtype comprising the hth discovered HA protein and the nth discovered NA protein. Influenza viruses A, B and C are very similar in overall structure. The viral particles of all influenza viruses are similar in composition. These are made of a viral envelope containing two main types of glycoproteins, wrapped around a central core. The central core contains the viral RNA genome and other viral proteins that package and protect this RNA. The influenza A genome contains 11 genes on eight pieces of RNA, encoding for 11 proteins: Hemagglutinin (HA), Neuraminidase (NA), Nucleoprotein (NP), M1, M2, NS1, NS2(NEP), PA, PB1, PB1-F2 and PB2.
Influenza A virus nucleoprotein (NP) forms homo-oligomers and multiple copies of NP wrap around genomic RNA, along with a trimeric polymerase making up ribonucleoprotein (RNP) complex. NP is composed of a head and a body domain and a tail loop / linker region. The head domain is more conserved than the body domain. NP oligomerization is mediated by the insertion of the non-polymorphic and structurally conserved tail loop of one NP molecule to a groove of another NP. The different form of NP oligomers is due to the flexibility of the polymorphic linkers that join the tail loop to the rest of the protein. The RNA binding property of NP is known to involve the protruding element and the flexible basic loop between the head and body domains, both having high degree of primary sequence conservation.

 

References

  1. Li KS, et al., 2004, Nature. 430: 209-13.
  2. Epstein, S.L. et al., 2005, Vaccine. 23 (46-47): 5404-10.
  3. Christophe F, et al., 2009, Science. 324: 1557-61.
  4. Guan Y, et al., 2009, Revue scientifique et technique. 23(2): 453-65.
  5. Ng, A.K. et al., 2009, Sci China C Life Sci. 52 (5):439-49.               
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