Peptides & Amino Acids

The FLAG® peptide (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys or DYKDDDDK) is intended for immunoaffinity chromatography to allow elution under non-denaturing conditions by competitive elution with excess of free FLAG® Peptide.

The Triple FLAG® Peptide is a synthetic peptide of 23 amino acid residues (molecular weight of 2861.9 daltons). The Asp-Tyr-Lys-Xaa-Xaa-Asp motif is repeated three times in the peptide. Eight amino acids at the C-terminus make up the classic FLAG® sequence (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys or DYKDDDDK). The triple FLAG peptide is intended for immunoaffinity chromatography to allow elution under non-denaturing conditions by competitive elution with excess of free triple FLAG® Peptide.

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

Apelin (APLN) is an endogenous ligand for APJ, an alternative coreceptor with CD4 for HIV-1 infection. It inhibits HIV-1 entry in cells coexpressing CD4 and APJ. It is widely expressed in various organs. Apelin-36 has a greater inhibitory activity on HIV infection than other synthetic apelin derivatives. The oral intake in the colostrum and the milk could have a role in the modulation of the immune responses in neonates. May also have a role in the central control of body fluid homeostasis by influencing AVP release and drinking behavior. Recently, 46 different apelin peptides ranging from apelin 55 (proapelin) to apelin 12 have been identified in bovine colostrum.

Apelin (APLN) is an endogenous ligand for APJ, an alternative coreceptor with CD4 for HIV-1 infection. It inhibits HIV-1 entry in cells coexpressing CD4 and APJ. It is widely expressed in various organs. Apelin-36 has a greater inhibitory activity on HIV infection than other synthetic apelin derivatives. The oral intake in the colostrum and the milk could have a role in the modulation of the immune responses in neonates. May also have a role in the central control of body fluid homeostasis by influencing AVP release and drinking behavior. Recently, 46 different apelin peptides ranging from apelin 55 (proapelin) to apelin 12 have been identified in bovine colostrum.

Apelin (APLN) is an endogenous ligand for APJ, an alternative coreceptor with CD4 for HIV-1 infection. It inhibits HIV-1 entry in cells coexpressing CD4 and APJ. It is widely expressed in various organs. Apelin-36 has a greater inhibitory activity on HIV infection than other synthetic apelin derivatives. The oral intake in the colostrum and the milk could have a role in the modulation of the immune responses in neonates. May also have a role in the central control of body fluid homeostasis by influencing AVP release and drinking behavior. Recently, 46 different apelin peptides ranging from apelin 55 (proapelin) to apelin 12 have been identified in bovine colostrum.

Parathyroid hormone (pTH) is the most important endocrine regulator of Ca2+ and phosphorus concentration in the extracellular fluid. pTH is secreted from cells of the parathyroid glands and acts for the most part via the binding to specific G-protein coupled receptors on the surface of  target cells in bone and kidney, utilizing the second messenger adenylate cyclase to regulate cAMP levels in cells.  Like most other protein hormones, parathyroid hormone is synthesized as a preprohormone and is processed intracellularly.  The mature hormone, 84 amino acids in length, is released from secretory vesicles into the blood.  Biologic effects of large C-terminal parathyroid hormone (PTH) fragments, such as pTH 7-84, are thought to regulate PTH secretion via an autocrine/paracrine regulatory mechanism

Parathyroid hormone (pTH) is the most important endocrine regulator of Ca2+ and phosphorus concentration in the extracellular fluid. pTH is secreted from cells of the parathyroid glands and acts for the most part via the binding to specific G-protein coupled receptors on the surface of  target cells in bone and kidney, utilizing the second messenger adenylate cyclase to regulate cAMP levels in cells.  Like most other protein hormones, parathyroid hormone is synthesized as a preprohormone and is processed intracellularly.  The mature hormone, 84 amino acids in length, is released from secretory vesicles into the blood.  Biologic effects of large C-terminal parathyroid hormone (PTH) fragments, such as pTH 7-84, are thought to regulate PTH secretion via an autocrine/paracrine regulatory mechanism