314 Results for: "peptide synthesis"

Supplier: Biotium

This antibody recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

This antibody recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

This antibody recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein L gene family encodes six highly homologous proteins designated apoL-I to -VI, which are associated with large high density type lipoproteins (HDL) (2,3). The human apoL family maps to chromosome 22q12.1-13.1 within a 127,000-bp region (4). ApoL has been characterized as a pancreas specific, 383-amino acid protein that contains a 12-amino acid secretory signal peptide (4). The apoL genes have TATA-less promoters and contain putative sterol regulatory elements, suggesting that transcription of these genes may be coordinated with that of the low density lipoprotein receptor and genes in pathways involving the synthesis of triglycerides and cholesterol (3). ApoL homologs can undergo 10 fold changes in expression during atherosclerotic changes in vascular endothelial cells, which includes the inflammatory reaction of atherosclerotic lesions (5).

Supplier: Cayman Chemical

Protein arginine deiminase 6 (PAD6) is a homodimeric guanidine-modifying enzyme belonging to the amidinotransferase superfamily. It is a calcium-dependent enzyme that catalyzes the post-translational modification of target proteins by converting arginine to citrulline. PAD6 is expressed in mammalian oocytes, sperm cells, and early embryos. In mammalian oocytes and early embryo cytoplasm, its expression is localized to cytoskeletal sheets, dynamic structures containing various keratins, which are major targets for citrullination. PAD6-/- oocytes exhibit reduced microtubule acetylation and defective organelle positioning and redistribution, suggesting a role for PAD6 in regulating microtubule-mediated organelle movement and positioning. PAD6-/- female, but not male, mice are infertile due to a reduction of de novo protein synthesis, cytoskeletal sheet formation, and ribosomal RNA which induces arrest of zygote development at the two-cell stage. PAD6 is regulated by newborn ovary homeobox (Nobox), as its promoter contains a Nobox DNA-binding element (NBE) and expression and activity of PAD6 are decreased in Nobox-/- mouse ovaries.5 In human females, homozygous nonsense mutations and compound-heterozygous mutations in PAD6 induce early embryonic arrest following in vitro fertilization (IVF) or intracytoplasmic sperm injection (ICSI).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein L gene family encodes six highly homologous proteins designated apoL-I to -VI, which are associated with large high density type lipoproteins (HDL) (2,3). The human apoL family maps to chromosome 22q12.1-13.1 within a 127,000-bp region (4). ApoL has been characterized as a pancreas specific, 383-amino acid protein that contains a 12-amino acid secretory signal peptide (4). The apoL genes have TATA-less promoters and contain putative sterol regulatory elements, suggesting that transcription of these genes may be coordinated with that of the low density lipoprotein receptor and genes in pathways involving the synthesis of triglycerides and cholesterol (3). ApoL homologs can undergo 10 fold changes in expression during atherosclerotic changes in vascular endothelial cells, which includes the inflammatory reaction of atherosclerotic lesions (5).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins. The apolipoprotein L gene family encodes six highly homologous proteins designated apoL-I to -VI, which are associated with large high density type lipoproteins (HDL). The human apoL family maps to chromosome 22q12.1-13.1 within a 127,000-bp region. ApoL has been characterised as a pancreas specific, 383-amino acid protein that contains a 12-amino acid secretory signal peptide. The apoL genes have TATA-less promoters and contain putative sterol regulatory elements, suggesting that transcription of these genes may be coordinated with that of the low density lipoprotein receptor and genes in pathways involving the synthesis of triglycerides and cholesterol. ApoL homologs can undergo 10 fold changes in expression during atherosclerotic changes in vascular endothelial cells, which includes the inflammatory reaction of atherosclerotic lesions.

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein L gene family encodes six highly homologous proteins designated apoL-I to -VI, which are associated with large high density type lipoproteins (HDL) (2,3). The human apoL family maps to chromosome 22q12.1-13.1 within a 127,000-bp region (4). ApoL has been characterized as a pancreas specific, 383-amino acid protein that contains a 12-amino acid secretory signal peptide (4). The apoL genes have TATA-less promoters and contain putative sterol regulatory elements, suggesting that transcription of these genes may be coordinated with that of the low density lipoprotein receptor and genes in pathways involving the synthesis of triglycerides and cholesterol (3). ApoL homologs can undergo 10 fold changes in expression during atherosclerotic changes in vascular endothelial cells, which includes the inflammatory reaction of atherosclerotic lesions (5).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein L gene family encodes six highly homologous proteins designated apoL-I to -VI, which are associated with large high density type lipoproteins (HDL) (2,3). The human apoL family maps to chromosome 22q12.1-13.1 within a 127,000-bp region (4). ApoL has been characterized as a pancreas specific, 383-amino acid protein that contains a 12-amino acid secretory signal peptide (4). The apoL genes have TATA-less promoters and contain putative sterol regulatory elements, suggesting that transcription of these genes may be coordinated with that of the low density lipoprotein receptor and genes in pathways involving the synthesis of triglycerides and cholesterol (3). ApoL homologs can undergo 10 fold changes in expression during atherosclerotic changes in vascular endothelial cells, which includes the inflammatory reaction of atherosclerotic lesions (5).

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.

Supplier: Bioss

Human reproduction is controlled by the hypothalaic-pituitary gonadal axis laid down early in fetal development. Gonadotropin releasing hormone (GnRH), also known as GnRH-associated peptide, luteinizing hormone releasing hormone (LHRH), luliberin or gonadorelin, is a decapeptide that is an important molecule in the hypothalamic-pituitary-gonadal axis control circuit. GnRH is produced by hypothalamic neurons and secreted in a pulsatile manner into the capillary plexus of the medianeminence. GnRH affects the release of lutenizing hormone and follicle stimulating hormone from gonadotropic cells in the anterior pituitary. In addition to hypothalamic GnRH (GnRH I), a second GnRH form (GnRH II) functions primarily in the midbrain. GnRH is expressed in the acrosomal region of human sperm and in the anterior pituitary tissue and cancer cells. Unlike GnRH I, GnRH II is highly expressed outside the brain, particularly in the kidney, bone marrow and prostate, suggesting that it may have multiple functions. GnRH binds to a specific G protein-coupled receptor in the pituitary to regulate synthesis and secretion of gonadotropins.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.