"Biosensis"

Supplier: Biosensis

Peptide YY (PYY) is secreted from endocrine cells in the lower small intestine, colon and pancreas. PYY inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility (Ref: SWISS-Prot).

Supplier: Biosensis

C-reactive protein has several roles associated with host defence such as; promoting agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. It can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. COFACTOR: Binds 2 calcium ions per subunit. C-reactive protein exists as a homopentamer. There are 2 alternatively spliced isoforms. C-reactive protein is found in plasma and its concentration increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli. It is induced by IL-1 and IL-6.

Supplier: Biosensis

Transforming growth factor beta-1 (TGFB1) is a multi-functional cytokine with roles in proliferation, differentiation and other functions in many cell types. The secreted TGFB1 protein is cleaved into a latency-associated peptide (LAP) and a mature TGFB1 peptide (Ref: SWISS-Prot).

Supplier: Biosensis

Uncoupling Protein 3 (UCP3) belongs to the mitochondrial carrier family. Located in the mitochondrion inner membrane, UCP3 creates proton leaks across the membrane thus uncoupling oxidative phosphorylation (Ref: SWISSPROT).

Supplier: Biosensis

Dicer is the rate limiting enzyme in the formation of mature microRNAs.

Supplier: Biosensis

FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons. SUBUNIT: Homodimer, associated by noncovalent forces. SUBCELLULAR LOCATION: Secreted protein. SIMILARITY: Belongs to the NGF-beta family.

Supplier: Biosensis

The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).

Supplier: Biosensis

The heat shock proteins were discovered, as the name suggests, since they are heavily upregulated when cells are stressed by temperatures above the normal physiological range. They are expressed in unstressed cells also and have a normal function as chaperones, helping other proteins to fold correctly, and are required in much greater amounts if the cell or tissue is stressed by heat. The increased levels are generated transcriptionally under the influence of a powerful transcription factor, the heat shock factor 1 (HSF1). The different heat shock proteins were originally named based on their SDS-PAGE mobility, so HSP27 has an apparent molecular weight of 27kDa. It is an abundant protein even under non-stress conditions and frequently shows up as a major spot on 2 dimensional gels of cells or tissues. It is known to associate with a variety of other proteins such as actin, intermediate filament subunits and ubiquitin and is found both in the cytoplasm and the nucleus of cells. HSP27 can become heavily phosphorylated under the influence of multiple protein kinases particularly as a result of activation of the p38/SAPK pathway. Upregulation of this protein is protective against neurodegenerative diseases at least in certain mouse models (1). Point mutations in the HSP27 gene are associated with two neurological diseases, Charcot-Marie-Tooth disease type 2F and distal hereditary motor neuropathy IIB (2). These diseases are associated with axonal loss apparently following defects in the transport of neurofilaments.

Supplier: Biosensis

Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. COFACTOR: Binds 2 calcium ions per subunit.

Supplier: Biosensis

FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons. SUBUNIT: Homodimer, associated by noncovalent forces. SUBCELLULAR LOCATION: Secreted protein. SIMILARITY: Belongs to the NGF-beta family.

Supplier: Biosensis

AGRP is the endogenous antagonist of alpha-melanocyte stimulating hormone and has been shown to cause potent stimulation of food intake, and this protein is found in over 90% of Neuropeptide Y containing cells in rats.

Supplier: Biosensis

Proopiomelanocortin (POMC) is the precursor of the melanocortin peptides alpha, beta and gamma. POMC neurons in the arcuate nucleus of the hypothalamus function as key central regulators of food intake and homeostatic control of energy balance in both rodents and non-human primates. MSH increases the pigmentation of skin by increasing the melanin production in melanocytes. MSH is produced in the pituitary gland and belongs to the POMC family.

Supplier: Biosensis

Proopiomelanocortin (POMC) is the precursor of the melanocortin peptides alpha, beta and gamma. POMC neurons in the arcuate nucleus of the hypothalamus function as key central regulators of food intake and homeostatic control of energy balance in both rodents and non-human primates.

Supplier: Biosensis

Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR) and upon binding to the receptor it induces the release of growth hormone from the pituitary. This ligand has an appetite-stimulating effect and is involved in growth regulation.

Supplier: Biosensis

Luteinizing hormone promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. It exists as a heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin, and gonatropin.

Supplier: Biosensis

Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. It belongs to the vasopressin/oxytocin family. Oxytocin is secreted.