Proteins

Parathyroid Hormone (PTH) is the most important endocrine regulator of calcium and phosphorus con- centration in extracellular fluid. Parathyroid Hormone (PTH) is secreted from cells of the parathyroid glands and finds Parathyroid Hormone’s major target cells in bone and kidney. Like most other protein hormones, Parathyroid Hormone (PTH) is synthesized as a preprohormone. After intracellular processing, the mature hormone is packaged within the Golgi into secretory vesicles, the secreted into blood by exocytosis. Parathyroid Hormone (PTH) is secreted as a linear protein of 84 amino acids. Recombinant Human Parathyroid Hormone (PTH) produced in E. coli is a single, non-glycosylated, polypeptide chain containing 84 amino acids.

Polypeptide hormones secreted by the parathyroid glands, which promote release of calcium from bone to extracellular fluid by activating osteoblasts and inhibiting osteoclasts, indirectly promote increased intestinal absorption of calcium, and promote renal tubular reabsorption of calcium and increased renal excretion of phosphates. It is a major regulator of bone metabolism. Secretion of parathyroid hormone increases when the level of calcium in the extracellular fluid is low. Its action is opposed by calcitonin.

Polypeptide hormones secreted by the parathyroid glands, which promote release of calcium from bone to extracellular fluid by activating osteoblasts and inhibiting osteoclasts, indirectly promote increased intestinal absorption of calcium, and promote renal tubular reabsorption of calcium and increased renal excretion of phosphates. It is a major regulator of bone metabolism. Secretion of parathyroid hormone increases when the level of calcium in the extracellular fluid is low. Its action is opposed by calcitonin.

PVR is a Type I transmembrane glycoprotein in the immunoglobulin superfamily. Commonly known as Poliovirus Receptor (PVR) due to its involvement in the cellular poliovirus infection in primates. PVR’s normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells. PVR/CD155 was originally isolated based on its ability to mediate polio virus attachment to host cells. The full length (or PVR alpha isoform) is synthesized as a 417 amino acid (aa) precursor that contains a 20aa signal sequence, a 323aa extracellular region, a 24aa TM segment and a 50aa cytoplasmic tail. PVR binds other molecules including Vitronectin, Nectin-3, DNAM-1/CD226, CD96, and TIGIT but does not bind homotypically. PVR is up-regulated on endothelial cells by IFN-gamma and is highly expressed on immature thymocytes, lymph node dendritic cells, and tumor cells of epithelial and neuronal origin.

PVR is a Type I transmembrane glycoprotein in the immunoglobulin superfamily. Commonly known as Poliovirus Receptor (PVR) due to its involvement in the cellular poliovirus infection in primates. PVR’s normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells. PVR/CD155 was originally isolated based on its ability to mediate polio virus attachment to host cells. The full length (or PVR alpha isoform) is synthesized as a 417 amino acid (aa) precursor that contains a 20aa signal sequence, a 323aa extracellular region, a 24aa TM segment and a 50aa cytoplasmic tail. PVR binds other molecules including Vitronectin, Nectin-3, DNAM-1/CD226, CD96, and TIGIT but does not bind homotypically. PVR is up-regulated on endothelial cells by IFN-gamma and is highly expressed on immature thymocytes, lymph node dendritic cells, and tumor cells of epithelial and neuronal origin.

CCL5 or RANTES (acronym for Regulated upon Activation, Normal T cell Expressed and presumably Secreted), was initially discovered by subtractive hybridization as a transcript expressed in T cells but not B cells. Eosinophilchemotactic activities released by thrombinstimulated human platelets have also been purified and found to be identical to RANTES. Besides T cells and platelets, RANTES has been reported to be produced by renal tubular epithelium, synovial fibroblasts and selected tumor cells.

CCL5 or RANTES (acronym for Regulated upon Activation, Normal T cell Expressed and presumably Secreted), was initially discovered by subtractive hybridization as a transcript expressed in T cells but not B cells. Eosinophilchemotactic activities released by thrombinstimulated human platelets have also been purified and found to be identical to RANTES. Besides T cells and platelets, RANTES has been reported to be produced by renal tubular epithelium, synovial fibroblasts and selected tumor cells.

Chemokine (C-C motif) ligand 5(CCL5), also known as RANTES (Regulated upon activation, Normal T cell Expressed and presumable Secreted) is a CC-chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. RANTES is chemotactic for T cells, eosinophils, and basophils, and plays an active role in recruiting leukocytes in inflammatory sites. With the help of specific cytokines (i.e., IL-2 and IFN-γ) that are released by T cells, RANTES induces the proliferation and activation of certain natural-killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. RANTES is also an HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans. It has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV).

Chemokine (C-C motif) ligand 5(CCL5), also known as RANTES (Regulated upon activation, Normal T cell Expressed and presumable Secreted) is a CC-chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. RANTES is chemotactic for T cells, eosinophils, and basophils, and plays an active role in recruiting leukocytes in inflammatory sites. With the help of specific cytokines (i.e., IL-2 and IFN-γ) that are released by T cells, RANTES induces the proliferation and activation of certain natural-killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. RANTES is also an HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans. It has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV).

The properties of retinol binding protein is the transport carrier of vitamin A in the plasma. Human-retinol binding protein is a single-chain polypeptide with a molecular weight of approximately 21000 and one binding site for retinol and other forms of vitamin A. In addition, compounds related to retinol, such as retinal, retinoic acid, retinyl esters and geometric isomers of retinol and of retinal were evaluated for their ability to bind to this protein. In plasma, RBP4-retinol forms a complex with transthyretin (TTR), also known as thyroxine-binding protein and prealbumin. Defects in RBP4 cause retinol-binding protein deficiency, which affects night vision.

The properties of retinol binding protein is the transport carrier of vitamin A in the plasma. Human-retinol binding protein is a single-chain polypeptide with a molecular weight of approximately 21000 and one binding site for retinol and other forms of vitamin A. In addition, compounds related to retinol, such as retinal, retinoic acid, retinyl esters and geometric isomers of retinol and of retinal were evaluated for their ability to bind to this protein. In plasma, RBP4-retinol forms a complex with transthyretin (TTR), also known as thyroxine-binding protein and prealbumin. Defects in RBP4 cause retinol-binding protein deficiency, which affects night vision.

The properties of retinol binding protein is the transport carrier of vitamin A in the plasma. Human-retinol binding protein is a single-chain polypeptide with a molecular weight of approximately 21000 and one binding site for retinol and other forms of vitamin A. In addition, compounds related to retinol, such as retinal, retinoic acid, retinyl esters and geometric isomers of retinol and of retinal were evaluated for their ability to bind to this protein. In plasma, RBP4-retinol forms a complex with transthyretin (TTR), also known as thyroxine-binding protein and prealbumin. Defects in RBP4 cause retinol-binding protein deficiency, which affects night vision.

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