p39 蛋白

Application Note: p39 is suitable as a control in immunological assays. Specific conditions for reactivity should be optimized by the end user. Expect a band at 77.8 kDa for p39-MBP, (35.4 kDa for p39 and 42.4 kDa for MBP) in size corresponding to p39 by Western blotting in the appropriate cell lysate or extract. p39 protein was tested in SDS-page and western blot.

Western Blot Dilution: User Optimized

ELISA Dilution: User Optimized

Other: Lateral Flow Assay: User Optimized

Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

Stabilizer: None

Synonyms: Basic membrane protein A, Borrelia burgdorferi bmpA, immunodominant antigen P39, membrane lipoprotein BmpA, control protein

Background: The p39 protein, or Basic membrane protein A, is one of the immunogenic cell membrane components of Borrelia burgdorferi, the spirochete carried by Ixodes ticks. The spirochete migrates from the tick midgut during feeding to its salivary glands and are thus transmitted to the mammal host. This transition may be facilitated by changes in expression of some B. burgdorferi genes. It is believed that expression of the various proteins associated with the spirochete may be regulated by the changes in tick life cycle, changes in conditions during tick feeding (such as temperature, pH , and nutrients) and/or in coordination with the course of infection of the mammal host. BmpA is expressed during the invasion of the spirochete and in the evolution of the arthritis of Lyme disease in mammals. It belongs to the BMP lipoprotein family. The major products of the B. burgdorferi basic membrane protein (bmp) A/B operon that are induced in murine and human joints possess inflammatory properties. Non-lipidated and lipidated versions of BmpA have been shown to induce the pro-inflammatory cytokine TNF-α and IL-1ß in human synovial cells. The induction of cytokine responses in synovial cells via activation of the NF-kappaB and p38 MAP kinase pathways could potentially contribute to the genesis of Lyme arthritis. The BmpA outer-surface protein is an important antigen for serodiagnosis of human infection. B. burgdorferi adheres to host extracellular matrix components, including laminin, but may not bind mammalian type I or type IV collagens or fibronectin. Lyme disease proteins are ideal for researchers interested in immunology, neurology, rheumatology, coinfections, autoimmune, and neurodegenerative diseases.