prion antibody and antigen (recombinant protein)

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Diagnostic anti-prion antibodies pairs and antigen for animal health (animal Bovines/Cattle infectious disease Chronic wasting disease) 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-P281-Ag01	Recombinant prion protein	$3090.00
GMP-VT-P281-Ab01	Anti-prion mouse monoclonal antibody (mAb)	$3090.00
GMP-VT-P281-Ab02	Anti-prion mouse monoclonal antibody (mAb)	$3090.00

Size： 1mg | 10mg | 100mg

Product Description

Cat No.	GMP-VT-P281-Ag01
Product Name	Recombinant prion protein
Pathogen	prion
Expression platform	E.coli
Isotypes	Recombinant Antigen
Bioactivity validation	Anti-prion antibodies binding, Immunogen in Sandwich Elisa, lateral-flow tests, and other immunoassays as control material in prion level test of animal Bovines/Cattle infectious disease with Chronic wasting disease.
Tag	His
Product description	Recombinant prion 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 GM's Protein Stability Buffer2 (PSB2,Confidential Ingredients) or PBS (pH7.4); For PSB2, reconstituted with 0.9% sodium chloride; For PBS, reconstituted with ddH2O.
Storage	Store at -20℃ to -80℃ under sterile conditions. Avoid repeated freeze-thaw cycles.

Cat No.	GMP-VT-P281-Ab01,GMP-VT-P281-Ab02
Pathogen	prion
Product Name	Anti-prion mouse monoclonal antibody (mAb)
Expression platform	CHO
Isotypes	Mouse IgG
Bioactivity validation	Recombinant prion antigen binding, ELISA validated as capture antibody and detection antibody. Pair recommendation with other anti-prion antibodies in prion level test of animal Bovines/Cattle infectious disease with Chronic wasting disease.
Product description	Anti-prion 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-prion antibodies./td>
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 GM's Protein Stability Buffer2 (PSB2,Confidential Ingredients) or PBS (pH7.4); For PSB2, reconstituted with 0.9% sodium chloride; For PBS, reconstituted with ddH2O.
Storage	Store at -20℃ to -80℃ under sterile conditions. Avoid repeated freeze-thaw cycles.

Reference

Validation Data

Click to get more Data / Case study about the product.

Pathogen

Prions, also known as proteinaceous infectious particles, are intriguing and enigmatic infectious agents that continue to inspire significant research interest due to their unusual properties. Unlike other classical pathogens such as viruses, bacteria, fungi, and parasites, prions do not possess a genome or an outer shell. Instead, they consist solely of abnormally folded forms of a normal cellular protein, known as the prion protein (PrP). The PrP protein is predominantly expressed in neurons and is essential for normal synaptic function, although its precise physiological role is not fully understood.

A defining characteristic of prions is their ability to propagate themselves by inducing normal, non-pathogenic PrP molecules to refold into the same conformation as the misfolded protein. This process, known as template-assisted propagation, results in the accumulation of aggregates of misfolded PrP molecules that are resistant to degradation and are thought to be responsible for the neurotoxicity observed in prion diseases. Although prions are typically thought of as being neurotoxic, recent research suggests that these proteins may have additional roles in other tissues and biological processes. For example, recent studies have suggested that PrP may play a role in regulating hematopoietic stem cell proliferation.

Prion diseases are rare, transmissible, and fatal neurodegenerative disorders that affect humans and other mammals. These diseases are characterized by the accumulation of abnormally-folded PrP in the central nervous system (CNS), leading to the destruction of neurons and the subsequent development of clinical symptoms such as dementia, ataxia, and myoclonus. The most common form of human prion disease is sporadic Creutzfeldt-Jakob disease, which affects approximately 1 in 1 million people worldwide. Other forms of prion disease include genetic or familial forms of CJD, variant CJD (vCJD), and Gerstmann-Straussler-Scheinker syndrome (GSS). In addition to these human prion diseases, prion diseases have been identified in a variety of other animal species, including bovine spongiform encephalopathy and chronic wasting disease in deer and elk.

Diagnostic methods for prion diseases typically involve analyzing samples of cerebrospinal fluid or brain tissue to detect abnormal levels of PrP protein or to identify specific types of PrP that are associated with prion diseases. These methods may include western blotting, immunohistochemistry, and enzyme-linked immunosorbent assays (ELISA), which can target specific regions or isoforms of PrP protein. In addition, nucleic acid-based techniques such as RT-QuIC and real-time PCR may also be used to detect abnormal forms of the PrP gene.

The management of prion diseases currently relies largely on supportive care, including symptom management and palliative measures. However, there is significant ongoing research aimed at developing effective treatments for prion diseases, including small molecule inhibitors of PrP aggregation, immunotherapy approaches targeting PrP, and gene editing techniques to correct mutations in the PRNP gene associated with genetic forms of prion disease.

In conclusion, prions are a unique and challenging class of infectious agents that continue to captivate scientific interest due to their unusual properties and devastating impact on human and animal health. Although much remains to be understood about the biology of prions and the pathogenesis of prion diseases, ongoing research efforts hold promise for the development of effective treatments for these rare and lethal disorders.

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