Patents
Literature
Hiro is an intelligent assistant for R&D personnel, combined with Patent DNA, to facilitate innovative research.
Hiro

78 results about "Myelin sheath structure" patented technology

The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of axonal impulse conduction. MBP maintains the correct structure of myelin, interacting with the lipids in the myelin membrane.

Peptide specificity of anti-myelin basic protein and the administration of myelin basic protein peptides to multiple sclerosis patients

Human myelin basic protein (h-MBP) has a molecular weight of 18.5 KD and contains 170 amino acid residues. Synthetic peptides ranging in length from about 8 to 25 residues and covering the entire length of the protein have been produced. Antibodies to h-MBP (anti-MBP) were found to be neutralized by the synthetic peptides, in vitro, which span the h-MBP from about amino acid residue 61 to about amino acid residue 106. The peptides, which cover both the amino (about residues 1 to 63) and carboxy (about residues 117 to 162) terminals of h-MBP did not neutralize purified anti-MBP. Intrathecal administratin of peptide MBP(75-95), MBP(86-95), or MBP(82-98) produced complete binding-neutralization of free (F) anti-MBP with no change in bound (B) levels. A control peptide MBP35-58 had no effect on F or B anti-MBP levels. Intravenous administration of MBP(75-95), MBP(86-95), or MBP(82-98) resulted in significant decline of F and B CSF anti-MBP levels. Administration of MBP synthetic peptides to MS patients either intrathecally or intravenously did not have any adverse neurological effects and systemic complications did not occur. The MBP epitope for MS anti-MBP has been localized to an area between amino acid 86 and amino acid 95.
Owner:ALBERTA THE GOVERNORS OF THE UNIV

Method for preparing pre-staining luminescent protein marker

The invention provides a method for preparing a pre-staining luminescent protein marker. The method comprises the following steps: acquiring a protein A gene, a protein G gene, an MBP (Myelin Basic Protein) gene and a heavy chain constant region gene (CH gene) of a mouse and rabbit derived antibody, and cutting and combining the genes according to sizes of different proteins in a pre-staining luminescent protein marker; expressing the proteins, purifying, and mixing proteins of different molecule weights according to a certain ratio so as to obtain a luminescent protein marker; mixing the prepared luminescent protein marker with the pre-staining luminescent protein marker according to different ratios. The pre-staining luminescent protein marker prepared by using the method is capable of recognizing primary antibodies or secondary antibodies of different sources, binding sites of proteins are increased, light signals are intensified, not only are general positions of proteins indicated in the electrophoresis process and after membrane transfer, but also precise positions of the proteins can be indicated on X-ray films, no extra pre-staining marker channels are needed, no extra antibodies are needed, and the luminescent proteins can be combined with IgG or anti-rabbit and anti-mouse secondary antibodies derived from species such as human beings, rats, mice and rabbits.
Owner:南京赛诺博生物科技有限责任公司

Peptide specificity of anti-myelin basic protein and the administration of myelin basic protein peptides to multiple sclerosis patients

Human myelin basic protein (h-MBP) has a molecular weight of 18.5 KD and contains 170 amino acid residues. Synthetic peptides ranging in length from about 8 to 25 residues and covering the entire length of the protein have been produced. Antibodies to h-MBP (anti-MBP) were found to be neutralized by the synthetic peptides, in vitro, which span the h-MBP from about amino acid residue 61 to about amino acid residue 106. The peptides, which cover both the amino (about residues 1 to 63) and carboxy (about residues 117 to 162) terminals of h-MBP did not neutralize purified anti-MBP. Intrathecal administratin of peptide MBP(75-95), MBP(86-95), or MBP(82-98) produced complete binding-neutralization of free (F) anti-MBP with no change in bound (B) levels. A control peptide MBP35-58 had no effect on F or B anti-MBP levels. Intravenous administration of MBP(75-95), MBP(86-95), or MBP(82-98) resulted in significant decline of F and B CSF anti-MBP levels. Administration of MBP synthetic peptides to MS patients either intrathecally or intravenously did not have any adverse neurological effects and systemic complications did not occur. The MBP epitope for MS anti-MBP has been localized to an area between amino acid 86 and amino acid 95.
Owner:THE GOVERNORS OF THE UNIV OF ALBERTA
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products