Proteins & Peptides

Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a gut hormone. The biologically active forms of GLP-1 are GLP-1-(7-37) and GLP-1-(7-36) NH2. Those peptides result from selective cleavage of the proglucagon molecule.

Liraglutide is a human glucagon-like peptide-1 (GLP-1) agonist. GLP-1 (7-37) activates the GLP-1 cell-surface membrane-bound receptor in pancreatic beta cells. Liraglutide regulates insulin and glucagon secretions.

Myelin oligodendrocyte glycoprotein (MOG) is a minor constituent of the CNS myelin synthesized by oligodendrocytes and Schwann cells and is thought to mediate homophilic cell-cell adhesion among other roles. MOG, Myelin basic protein (MBP), and proteolipid proteins (PLP) are potential primary encephalitogenic target antigens in multiple sclerosis.

Myelin oligodendrocyte glycoprotein (MOG) is a minor constituent of the CNS myelin synthesized by oligodendrocytes and Schwann cells and is thought to mediate homophilic cell-cell adhesion among other roles. MOG, Myelin basic protein (MBP), and proteolipid proteins (PLP) are potential primary encephalitogenic target antigens in multiple sclerosis.

This peptide sequence corresponds to a class I (Kb)-restricted peptide epitope of OVA, an octameric peptide from ovalbumin presented by the class I MHC molecule, H-2Kb.

This peptide sequence corresponds to a class I (Kb)-restricted peptide epitope of OVA, an octameric peptide from ovalbumin presented by the class I MHC molecule, H-2Kb.

This peptide sequence corresponds to a class I (Kb)-restricted peptide epitope of OVA, an octameric peptide from ovalbumin presented by the class I MHC molecule, H-2Kb.

Translocation through the plasma membrane has been shown to be a major limiting step for the delivery of various macromolecules to the cytoplasm and other intracellular compartments (e.g., mitochondria, nucleus). Numerous studies have confirmed that specific peptide sequences known as cell penetrating peptides (CPP) derived from proteins able to cross the plasma membrane, can be added to various cargo and delivered across cell membranes. The cargo molecules that have been successfully transported into cells includes oligonucleotides, peptides, peptide nucleic acids, proteins and nanoparticles. One of these translocating peptides was derived from the HIV-1 Tat protein, specifically located within the first exon of the HIV tat protein. The specific HIV tat sequence is highly basic (cationic) and is readily added to peptides either as a preformed peptide with a site for direct conjugation to other molecules (typically a cysteine). Addition of the tat-cargo complex (5-50 uM concentrat

Translocation through the plasma membrane has been shown to be a major limiting step for the delivery of various macromolecules to the cytoplasm and other intracellular compartments (e.g., mitochondria, nucleus). Numerous studies have confirmed that specific peptide sequences known as cell penetrating peptides (CPP) derived from proteins able to cross the plasma membrane, can be added to various cargo and delivered across cell membranes. The cargo molecules that have been successfully transported into cells includes oligonucleotides, peptides, peptide nucleic acids, proteins and nanoparticles. One of these translocating peptides was derived from the HIV-1 Tat protein, specifically located within the first exon of the HIV tat protein. The specific HIV tat sequence is highly basic (cationic) and is readily added to peptides either as a preformed peptide with a site for direct conjugation to other molecules (typically a cysteine). Addition of the tat-cargo complex (5-50 uM concentrat