Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit antibody and antigen (recombinant protein)
Diagnostic anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit antibodies pairs and antigen for animal health (animal Avian/Bird/Poultry infectious disease Infectious bronchitis) testing in ELISA, colloidal gold-based Lateral flow immunoassay (LFIA), CLIA, TINIA and POCT
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Product information
Catalog No. | Description | US $ Price (per mg) |
---|---|---|
GMP-VT-P211-Tg001-Ag01 | Recombinant Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit protein | $3090.00 |
GMP-VT-P211-Tg001-Ab01 | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit mouse monoclonal antibody (mAb) | $3090.00 |
GMP-VT-P211-Tg001-Ab02 | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit mouse monoclonal antibody (mAb) | $3090.00 |
GMP-VT-P211-Tg001-Ab03 | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit human monoclonal antibody (mAb) | $3090.00 |
GMP-VT-P211-Tg001-Ab04 | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit human monoclonal antibody (mAb) | $3090.00 |
Size: 1mg | 10mg | 100mg
Product Description
Cat No. | GMP-VT-P211-Tg001-Ag01 |
Product Name | Recombinant Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit protein |
Pathogen | Infectious Bronchitis Virus - Variant 02 |
Expression platform | E.coli |
Isotypes | Recombinant Antigen |
Bioactivity validation | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit antibodies binding, Immunogen in Sandwich Elisa, lateral-flow tests, and other immunoassays as control material in Infectious Bronchitis Virus - Variant 02 level test of animal Avian/Bird/Poultry infectious disease with Infectious bronchitis. |
Tag | His | Product description | Recombinant Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit proteinwas expressed in E.coli - based prokaryotic cell expression system and is expressed with 6 HIS tag at the C-terminus. |
Purity | Purity: ≥95% (SDS-PAGE) |
Application | Paired antibody immunoassay validation in Sandwich ELISA, ELISA, colloidal gold-based Lateral flow immunoassay (LFIA), CLIA, TINIA, POCT and other immunoassays. |
Formulation | Lyophilized from sterile PBS, PH 7.4 |
Storage | Store at -20℃ to -80℃ under sterile conditions. Avoid repeated freeze-thaw cycles. |
Cat No. | GMP-VT-P211-Tg001-Ab01,GMP-VT-P211-Tg001-Ab02 |
Pathogen | Infectious Bronchitis Virus - Variant 02 |
Product Name | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit mouse monoclonal antibody (mAb) |
Expression platform | CHO |
Isotypes | Mouse IgG |
Bioactivity validation | Recombinant Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit antigen binding, ELISA validated as capture antibody and detection antibody. Pair recommendation with other anti-Infectious Bronchitis Virus - Variant 02 antibodies in Infectious Bronchitis Virus - Variant 02 level test of animal Avian/Bird/Poultry infectious disease with Infectious bronchitis. |
Product description | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit mouse monoclonal antibody (mAb) is a mouse monoclonal antibody produced by CHO technology. The antibody is ELISA validated as capture antibody and detection antibody. Pair recommendation with other anti-Infectious Bronchitis Virus - Variant 02 antibodies. |
Purity | Purity: ≥95% (SDS-PAGE) |
Application | Paired antibody immunoassay validation in Sandwich ELISA, ELISA, colloidal gold-based Lateral flow immunoassay (LFIA), CLIA, TINIA, POCT and other immunoassays. |
Formulation | Lyophilized from sterile PBS, PH 7.4 |
Storage | Store at -20℃ to -80℃ under sterile conditions. Avoid repeated freeze-thaw cycles. |
Cat No. | GMP-VT-P211-Tg001-Ab03,GMP-VT-P211-Tg001-Ab04 |
Pathogen | Infectious Bronchitis Virus - Variant 02 |
Product Name | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit human monoclonal antibody (mAb) |
Expression platform | CHO |
Isotypes | Human lgG1 |
Bioactivity validation | Recombinant Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit antigen binding, ELISA validated as capture antibody and detection antibody. Pair recommendation with other anti-Infectious Bronchitis Virus - Variant 02 antibodies in Infectious Bronchitis Virus - Variant 02 level test of animal Avian/Bird/Poultry infectious disease with Infectious bronchitis. |
Product description | Anti-Infectious Bronchitis Virus - Variant 02 spike glycoprotein, S2 subunit mouse monoclonal antibody (mAb) is a human monoclonal antibody produced by CHO. The antibody is ELISA validated as capture antibody and detection antibody pair. |
Purity | Purity: ≥95% (SDS-PAGE) |
Application | Paired antibody immunoassay validation in Sandwich ELISA, ELISA, colloidal gold-based Lateral flow immunoassay (LFIA), CLIA, TINIA, POCT and other immunoassays. |
Formulation | Lyophilized from sterile PBS, PH 7.4 |
Storage | Store at -20℃ to -80℃ under sterile conditions. Avoid repeated freeze-thaw cycles. |
Reference
Validation Data
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Pathogen Information
Erysipelothrix spp., a genus of Gram-positive, non-spore-forming bacteria, stands as a notable entity within the microbial landscape due to its diverse pathogenic capabilities. This taxonomically classified group falls within the class Erysipelotrichia, residing in the phylum Firmicutes. Characterized by its distinctive rod-shaped morphology, Erysipelothrix spp. has garnered scientific interest for its propensity to induce a spectrum of infections in both human and animal hosts. Among the species within this genus, Erysipelothrix rhusiopathiae emerges as a pivotal causative agent, prominently associated with a range of clinical manifestations.
The structural composition of Erysipelothrix spp. underpins its pathogenicity. While variations may exist among species, a commonality arises in the composition of their cell walls, primarily constituted by peptidoglycan. Within the intricate molecular architecture, the surface protective antigen SpaA assumes significance, particularly in Erysipelothrix rhusiopathiae. This protein, serving as a potential virulence factor, underscores the organism's adaptability and interaction with host environments.
Erysipelothrix spp. demonstrates a broad host range, infecting both humans and animals, with consequential diseases dictating its clinical significance. In the context of human infections, Erysipeloid emerges as a distinctive pathology. Typically contracted through direct contact with contaminated materials or animals, this affliction manifests as erythematous, swollen skin lesions, accompanied by localized pain. In the veterinary realm, swine and poultry represent susceptible hosts, showcasing the versatility of Erysipelothrix spp. in its ability to cross species barriers.
In the swine population, Erysipelothrix spp. exacts a toll through Swine Erysipelas. This multifaceted disease presents in varied forms, including the economically consequential diamond skin disease, acute septicemia, and chronic arthritis. The impact extends beyond the individual animal, affecting herd health and productivity. Poultry Erysipelas, on the other hand, affects chickens and turkeys, eliciting clinical signs such as dermatitis, septicemia, and joint swelling. The interconnectedness of these infections underscores the complex ecological niche occupied by Erysipelothrix spp. and its potential implications for agricultural and economic sectors.
Diagnostic endeavors for Erysipelothrix spp. infections encompass a multifaceted approach. Traditional culturing techniques involve the isolation of the bacterium from diverse clinical samples, including skin lesions and blood. The identification process relies on the nuanced interpretation of colony morphology and biochemical tests, providing a foundational understanding of the organism's presence. Molecular methods, particularly Polymerase Chain Reaction (PCR), amplify the diagnostic arsenal by targeting specific nucleic acid sequences. The rpoB gene, encoding the RNA polymerase beta subunit, serves as a focal point in such assays, offering both specificity and sensitivity in detecting Erysipelothrix spp.
Serological tests, notably Enzyme-Linked Immunosorbent Assay (ELISA), contribute to diagnostic precision by detecting antibodies against Erysipelothrix spp. in serum samples. This serodiagnostic approach aids in discerning the immune response to infection, guiding therapeutic interventions. Furthermore, genetic sequencing techniques unravel the genomic landscape of Erysipelothrix spp., facilitating not only confirmation of bacterial identity but also insights into the organism's evolution, virulence factors, and potential epidemiological implications.
In conclusion, Erysipelothrix spp. emerges as a captivating microbial entity, seamlessly navigating the complex interplay between hosts, diseases, and diagnostic modalities. Its significance spans across human and veterinary medicine, agricultural practices, and economic considerations. As scientific understanding evolves, the elucidation of Erysipelothrix spp.'s intricate molecular makeup and pathogenic intricacies promises to deepen our comprehension of microbial ecology and host-pathogen interactions.
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