Products

Nipah virus cDNA and Antigen

Cat#

Product Name

Swiss Prot#

Size

Price (US$)

Order

PN1250

Recombinant Protein-Nipah virus Nucleocapsid protein (a.a.51 to 532)

D2DEB7

100 µg

1195

Order

PN1251

Recombinant Protein-Nipah virus Glycoprotein G (a.a.71 to 602)

Q9IH62

100 µg

1195

Order

PN1252

Recombinant Protein-Nipah virus V protein (a.a.51 to 459)

Q4VCQ0

100 µg

1195

Order

PN1253

Recombinant Protein-Nipah virus Protein W (a.a.51 to 450)

P0C1C7

100 µg

1195

Order

PN1254

Recombinant Protein-Nipah virus C protein (a.a.21 to 166)

Q4VCP8

100 µg

1195

Order

PN1255

Recombinant Protein-Nipah virus Matrix protein (a.a.21 to 352)

D2DEB9

100 µg

1195

Order

PN1256

Recombinant Protein-Nipah virus RdRp catalytic (a.a.715 to 899)

Q997F0

100 µg

1195

Order

PN1257

Recombinant Protein-Nipah virus Nucleoprotein Protein N (a.a.31 to 332)

Q9IK92

100 µg

1195

Order

RPN1250

cDNA-Nipah virus Nucleocapsid protein (a.a.51 to 532)

D2DEB7

2 µg

2405

Order

RPN1251

cDNA-Nipah virus Glycoprotein G (a.a.71 to 602)

Q9IH62

2 µg

2655

Order

RPN1252

cDNA-Nipah virus V protein (a.a.51 to 459)

Q4VCQ0

2 µg

2040

Order

RPN1253

cDNA-Nipah virus Protein W (a.a.51 to 450)

P0C1C7

2 µg

1995

Order

RPN1254

cDNA-Nipah virus C protein (a.a.21 to 166)

Q4VCP8

2 µg

725

Order

RPN1255

cDNA-Nipah virus Matrix protein (a.a.21 to 352)

D2DEB9

2 µg

1655

Order

RPN1256

cDNA-Nipah virus RdRp catalytic (a.a.715 to 899)

Q997F0

2 µg

920

Order

RPN1257

cDNA-Nipah virus Nucleoprotein Protein N (a.a.31 to 332)

Q9IK92

2 µg

1505

Order

Nipah virus cDNA and recombinant antigen

  • Codon-optimized cDNA is cloned into E. coli expression vector with 6x His-tag at N-terminus and ready-to-use for recombinant protein production.
  • Recombinant protein applications: Western Blot may be used for other applications determined by the user.
  • Protein Purity: >90%, as determined by SDS-PAGE under reducing conditions.
  • Protein Activity: N/A
  • Protein Tag:  Contains A 6x histidine tag at N-terminus.
  • Protein Formulation: Liquid
  • Source: Produced from E. coli

Nipah virus is a highly infectious and deadly disease that primarily affects people and animals, particularly pigs. It was first identified in 1999 during an outbreak in Malaysia and Singapore. The virus is transmitted to humans from animals, especially bats, and from human to human through direct contact with bodily fluids. The symptoms of Nipah virus infection include fever, headache, drowsiness, respiratory illness, and encephalitis (inflammation of the brain). There is currently no specific treatment or vaccine for Nipah virus, and the disease can have a high mortality rate.

Nipah virus antigen refers to a substance that is specifically recognized and targeted by the immune system as being foreign or harmful. Antigens are typically proteins or other molecules found on the surface of viruses and bacteria, and they trigger an immune response. In the case of Nipah virus, the virus surface antigen can be used to develop diagnostic tests for the virus and to potentially design vaccines. By exposing the immune system to a specific antigen, it can learn to recognize and respond to the virus if it encounters it again in the future.

The Nipah virus genome is the genetic material of the virus, which contains all the information necessary for the virus to replicate and cause disease. The Nipah virus genome is a single strand of RNA (ribonucleic acid) that is about 19 kilobases in length. The genome codes for multiple proteins, including the envelope protein (which forms the virus envelope), the matrix protein (which is involved in virus assembly), and the nucleocapsid protein (which is involved in packaging the RNA genome). Understanding the Nipah virus genome is important for developing diagnostic tests, treatments, and vaccines for the virus. Studying the genome can also provide insights into the evolution and transmission of the virus.Here’s what you need to know about these proteins:

The Nucleocapsid protein is a structural protein that plays a crucial role in the virus’s life cycle. It helps to package and protect the virus’s genetic material and plays a role in the assembly and release of new virus particles.

The Glycoprotein G is another structural protein that is present on the surface of the virus. It is responsible for attaching the virus to host cells and facilitating entry into the cells. It is a major target for vaccine development and antiviral therapy.

The Protein (W, V, C) is a group of nonstructural proteins that are involved in the replication and transcription of the virus’s genetic material. These proteins interact with other viral proteins and host factors to facilitate the production of new virus particles.

The Matrix protein is a structural protein that is essential for the assembly and release of new virus particles. It plays a role in the formation of the virus’s outer envelope and is involved in the budding of new virus particles from infected cells.

The Nucleoprotein Protein N is a structural protein that interacts with the virus’s genetic material and helps to package it into a compact, organized structure within the virus particle. It is also involved in the replication and transcription of the virus’s genetic material.

Understanding the functions and interactions of these various proteins is critical for developing effective treatments and vaccines against the Nipah virus. Research in this area is ongoing, with the hope of finding new ways to prevent and treat this deadly disease.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.

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