H3N2 Canine, Mutant

Hemagglutinin-Influenza A Virus H3N2 Canine Recombinant, Mutant
Cat. No.
BT26091
Source

E. coli.

Synonyms
Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

H3N2 Canine produced in E. coli. is a single non-glycosylated polypeptide chain containing 336 amino acids (18-344) and having a molecular mass of 36.9kDa.
H3N2 Canine is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
H3N2, a subtype of influenza A virus, is named after its surface proteins hemagglutinin (H) and neuraminidase (N). This subtype undergoes genetic exchange with others, primarily for internal proteins. Historically, H3N2 has been more prevalent than H1N1, H1N2, and influenza B. Originating from H2N2 through antigenic shift, a process involving gene reassortment from multiple subtypes, both H2N2 and H3N2 acquired genes from avian influenza viruses. H3N2 can infect mammals and birds, with numerous strains emerging in pigs, humans, and birds due to mutations. Hemagglutinin (HA) facilitates viral attachment to host cells by binding to sialic acid-containing receptors on their surface. Playing a crucial role in host range restriction and virulence, HA enables viral entry into the cell's cytoplasm by mediating membrane fusion during endocytosis.
Description
Produced in E. coli, H3N2 Canine is a non-glycosylated polypeptide chain consisting of 336 amino acids (18-344), resulting in a molecular weight of 36.9kDa. This protein includes a 6 amino acid His-tag at the C-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The H3N2 Canine solution is provided at a concentration of 0.5mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For optimal stability, store the vial at 4°C if it will be used within 2-4 weeks. For extended storage, freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. It's important to minimize freeze-thaw cycles.
Purity
The purity of H3N2 Canine is determined to be greater than 95% using SDS-PAGE analysis.
Source

E. coli.

Amino Acid Sequence
ADNLPGNENN AATLCLGHHA VPNGTIVKTI TDDQIEVTNA TELVQNSSTG KICNNPHKIL DGRDCTLIDA LLGDPHCDVF QNETWDLFVE RSNAFSNCYP YDVPDYASLR SIVASSGTLE FITEGFTWAG VTQNGGSGAC KKGPANGFFS RLNWLTKSGN TYPVLNVTMP NNNNFDKLYI WGVHHPSTNQ EQTSLYIQAS GRVKVSTRRS QQTIIPNIGS RPLVRGQSGR ISVYWTIVKP GDVLVINSNG NLIAPRGYFK MRIGKSSIMR SDAPIDTCIS ECITPNGSIP NEKPFQNVNK ITYGACPKYV KQNTLKLATG MRNVPERQTH HHHHH

Product Science Overview

Introduction

Hemagglutinin (HA) is a glycoprotein found on the surface of the influenza viruses, playing a crucial role in the virus’s ability to infect host cells. The H3N2 subtype of the Influenza A virus has been a significant concern due to its ability to infect multiple species, including humans, birds, and dogs. The recombinant, mutant form of H3N2 canine influenza virus (CIV) has garnered attention due to its unique properties and implications for public health.

Hemagglutinin Structure and Function

Hemagglutinin is responsible for binding the virus to the host cell receptors, facilitating viral entry. It consists of two subunits: HA1 and HA2. The HA1 subunit contains the receptor-binding site, while the HA2 subunit is involved in the fusion of the viral and host cell membranes. Mutations in the HA protein can significantly alter the virus’s infectivity and antigenicity .

H3N2 Canine Influenza Virus

The H3N2 CIV was first identified in South Korea in 2007 and has since spread to other regions, including the United States. This virus is believed to have originated from avian influenza viruses and adapted to infect dogs. The H3N2 CIV poses a threat to public health due to its potential for cross-species transmission .

Recombinant and Mutant Forms

Recombinant H3N2 viruses are engineered to study the effects of specific mutations on the virus’s properties. These mutations can affect the virus’s ability to bind to host receptors, its thermal stability, and its antigenic properties. For example, the V223I substitution in the HA protein has been shown to reduce the virus’s binding affinity to human-type receptors while enhancing its thermal stability .

Implications for Public Health

The recombinant, mutant forms of H3N2 CIV are valuable tools for understanding the virus’s behavior and developing effective vaccines. Studies have shown that current human H3N2 vaccines do not confer protection against H3N2 CIVs, highlighting the need for continuous surveillance and vaccine development .

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