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Brand: ProteoGenix

Recombinant Chlamydia psittaci Porin/MOMP, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Chlamydia psittaci
Molecular weight:
42.49 kDa

$392.00

100ug + 392 loyalty points
Leu23–Phe391
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Recombinant Chlamydia psittaci Porin/MOMP, N-His

Recombinant Chlamydia psittaci Porin/MOMP, N-His

Product name Recombinant Chlamydia psittaci Porin/MOMP, N-His
Origin species Chlamydia psittaci
Expression system Prokaryotic expression
Molecular weight 42.49 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Leu23-Phe391
Aliases /Synonyms Major outer membrane porin, Porin, MOMP
Reference ARO-P12787
Note For research use only.
Molecular Constructor
Leu23–Phe391

Introduction

Recombinant Chlamydia psittaci Porin/MOMP (major outer membrane protein) is a highly conserved protein found in the outer membrane of the bacterium Chlamydia psittaci. This protein has been extensively studied for its potential use as a vaccine antigen and diagnostic tool for chlamydial infections. In this article, we will explore the structure, activity, and applications of this important recombinant protein.

Structure of Recombinant Chlamydia psittaci Porin/MOMP

The recombinant Chlamydia psittaci Porin/MOMP protein is a large, transmembrane protein consisting of approximately 400 amino acids. It is composed of four major domains: an N-terminal leader sequence, a conserved variable domain, a conserved membrane-spanning domain, and a C-terminal variable domain. The N-terminal leader sequence is responsible for targeting the protein to the outer membrane, while the variable domains are responsible for the protein’s antigenic variability.

The membrane-spanning domain is composed of hydrophobic amino acids and is responsible for anchoring the protein in the outer membrane. This domain also contains several conserved regions that are important for the protein’s function. Overall, the structure of recombinant Chlamydia psittaci Porin/MOMP is crucial for its activity and potential applications.

Activity of Recombinant Chlamydia psittaci Porin/MOMP

The main function of recombinant Chlamydia psittaci Porin/MOMP is to form pores in the outer membrane of the bacterium. These pores are important for the exchange of nutrients and waste products, as well as for the uptake of essential molecules from the host cell. Additionally, the protein has been shown to play a role in the attachment and invasion of host cells by chlamydial bacteria.

Furthermore, recombinant Chlamydia psittaci Porin/MOMP has been found to elicit a strong immune response in infected individuals. This is due to its high antigenicity and ability to induce both humoral and cellular immune responses. The protein has been shown to be a major target of the host’s immune system during chlamydial infections, making it a valuable tool for diagnostic purposes.

Applications of Recombinant Chlamydia psittaci Porin/MOMP

Recombinant Chlamydia psittaci Porin/MOMP has numerous potential applications in the field of chlamydial research and diagnostics. One of the most promising applications is its use as a vaccine antigen. Studies have shown that the protein can induce a strong and protective immune response, making it a potential candidate for a chlamydial vaccine. Furthermore, the protein’s conserved regions make it an attractive target for the development of a universal chlamydial vaccine that can protect against multiple strains of the bacteria.

Another potential application of recombinant Chlamydia psittaci Porin/MOMP is in the development of diagnostic tests. The protein’s high antigenicity and ability to induce a strong immune response make it an ideal candidate for the detection of chlamydial infections. Various immunoassays and serological tests have been developed using recombinant Porin/MOMP, which have shown high sensitivity and specificity for the detection of chlamydial infections.

Furthermore, recombinant Chlamydia psittaci Porin/MOMP has been used in research studies to better understand the pathogenesis of chlamydial infections. Its role in attachment and invasion of host cells, as well as its ability to elicit an immune response, have been extensively studied. This has led to a better understanding of the mechanisms involved in chlamydial infections, which can aid in the development of new treatment strategies.

Conclusion

Recombinant Chlamydia psittaci Porin/MOMP is a highly

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