"Bioss"

Supplier: Bioss

The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development. Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.

Supplier: Bioss

The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development. Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.

Supplier: Bioss

The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development. Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.

Supplier: Bioss

The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development. Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.

Supplier: Bioss

Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.

Supplier: Bioss

Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.

Supplier: Bioss

Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.

Supplier: Bioss

Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.

Supplier: Bioss

Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.

Supplier: Bioss

Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.

Supplier: Bioss

Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.

Supplier: Bioss

Contracts smooth muscle of the gastrointestinal and genitourinary tract, regulates growth hormone release, modulates insulin release, and may be involved in the control of adrenal secretion.

Supplier: Bioss

Insulysin was identified nearly a century ago as an enzyme responsible for the degradation of insulin in cells, although the precise interactions between insulin and insulysin remain elusive. Human insulysin was cloned in 1988, and shown to be a 118 kDa protein that exists primarily as a homodimer, and perhaps also complexed with other molecules. The sequence is well conserved between humans, rats and mice, and the antibody recognizes these species. Insulysin is a metalloproteinase of the clan ME, family M16, which contains an active site HxxEH, a reversal of the canonical HExxH zinc binding motif. Considered a zinc metalloproteinase, the activity of insulysin can be blocked with EDTA or 1-10 phenanthroline. In addition to the active metalloproteinase domain, insulysin contains a second metalloproteinase site which is considered catalytically inactive, and is thought to assist in substrate binding. Insulysin is most closely related to the bacterial proteinase pitrilysin, (the human orthologue of which appears to be MPRP1) and the mammalian proteinsae nardilysin. Generally thought to be a cytoplasmic protein, insulysin has been isolated from many different tissues and cell lines, and can degrade intact insulin, insulin B chain, glucagon, denatured hemoglobin, alpha amyloid protein, TGF alpha and amylin. Recent work implicates insulysin in clearing beta amyloid plaques from the brain, and has generated much interest in Alzheimer’s disease research. The pH optimum for insulysin is basic, pH 8.5, which also distinguishes it from other metalloproteinases. Insulin degrading enzyme (IDE) has a preferential affinity for insulin such that the presence of insulin will inhibit IDE mediated degradation of other substrates. IDE degrades a variety of other peptides including atrial natriuretic peptide and amylin.

Supplier: Bioss

Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.

Supplier: Bioss

Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.

Supplier: Bioss

Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.