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Description:
SGMS2 is a bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. SGMS2 directly and specifically recognizes the choline head group on the substrate. SGMS2 also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. SGMS2 does not function strictly as a SM synthase. SGMS2 is required for cell growth.Sphingomyelin (SM) is a major component of plasma membranes. It is preferentially concentrated in the outer leaflet and has a role in the formation of lipid rafts. SM synthases (EC 2.7.8.27), such as SGMS2, produce SM in the lumen of the Golgi and on the cell surface through the transfer of phosphocholine from phosphatidylcholine onto ceramide, yielding diacylglycerol as a side product (Huitema et al., 2004 [PubMed 14685263]).
Description:
Below 35 to 40 °C gelatin swells and absorbs approximately 5 to 10 times its weight of water to form a gel. Gelatin is soluble in glycerol and acetic acid, and more soluble in hot than in cold water. It is practically insoluble in most organic solvents such as alcohol, chloroform, carbon disulphide, carbon tetrachloride, ether, benzene, acetone and oils. Sterile solutions of gelatin stored cold are stable indefinitely, but at elevated temperatures hydrolysis or rupture of peptide bonds occurs, increasing the number of free amino groups. Gel strength and viscosity gradually weaken upon prolonged heating in solution above ~40 °C; this degradation is accelerated by extremes in pH, proteolytic enzymes and bacterial action.
Description:
Glycerol is a simple polyol compound which is a viscous liquid that is widely used in pharmaceutical formulations. It has three hydroxyl groups that are responsible for its solubility in water and its hygroscopic nature.
Description:
SGMS2 is a bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. SGMS2 directly and specifically recognizes the choline head group on the substrate. SGMS2 also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. SGMS2 does not function strictly as a SM synthase. SGMS2 is required for cell growth.Sphingomyelin (SM) is a major component of plasma membranes. It is preferentially concentrated in the outer leaflet and has a role in the formation of lipid rafts. SM synthases (EC 2.7.8.27), such as SGMS2, produce SM in the lumen of the Golgi and on the cell surface through the transfer of phosphocholine from phosphatidylcholine onto ceramide, yielding diacylglycerol as a side product (Huitema et al., 2004 [PubMed 14685263]).
Description:
Phospholipase A2(PLA2G1B) is a secreted protein which belongs to the phospholipase A2 family. It catalyses the release of fatty acids from glycero-3-phosphocholines. It catalyses the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules. Sequences of pancreatic PLA2G1B enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Mice lacking in PLA2G1B are resistant to obesity and diabetes induced by feeding a diabetogenic high-fat/high-carbohydrate diet. Oral supplementation of a diabetogenic diet with the PLA2G1B inhibitor methyl indoxam effectively suppresses diet-induced obesity and diabetes. PLA2G1B inhibition may be a potentially effective oral therapeutic option for treatment of obesity and diabetes.
Description:
Mouse Legumain,also known as LGMN, is a cysteine protease belonging to peptidase family C13 and is expressed in kidney and placenta abundantly. LGMN has a strict specificity for hydrolysis of asparaginyl bonds. It can also cleave aspartyl bonds slowly, especially under acidic conditions. The mammalian legumain is involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. It plays a role in the regulation of cell proliferation via its role in EGFR degradation. Legumain deficiency causes the accumulation of pro-Cathepsins B, H and L, another group of lysosomal cysteine proteases. Overexpression of Legumain in tumours is significant for invasion/metastasis. Mammalian legumain is inhibited by iodoacetamide and maleimides. Legumain activation appears to be autocatalytic and can be triggered by acidic pH.
Description:
Tumour necrosis factor (TNF, cachexin or cachectin and formerly known as tumour necrosis factor-alpha) is a cytokine involved in systemic inflammation and is a member of a group of cytokines that stimulate the acute phase reaction. The receptor TNF-R1 is activated by both the membrane-bound and soluble trimeric forms of TNF-alpha, whereas the receptor TNF-R2 only responds to the membrane-bound form of TNF-alpha (MultimericTNF-alpha (Prod. No. AG-40B-0019). Since the MultimericTNF-alpha mimics the membrane-bound form (forms oligomers higher than trimer), it is the only TNF-alpha protein that can activate the TNF-R2. For TNF-R1 activation, either "normal" TNF-alpha or MultimericTNF-alpha can be used."
Description:
Vascular endothelial growth factor A (VEGFA) is also known as Vascular permeability factor (VPF). VEGFA belongs to the PDGF/VEGF growth factor family. VEGFA is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Alternatively spliced transcript variants, encoding either freely secreted or cell-associated isoforms, have been characterized. VEGFA is produced by a group of three major isoforms as a result of alternative splicing and if any three isoforms are produced (VEGFA120, VEGFA164, and VEGFA188) then this will not result in vessel defects and death of the full VEGFA knockout in mice.
Description:
Vascular endothelial growth factor A (VEGFA) is also known as Vascular permeability factor (VPF). VEGFA belongs to the PDGF/VEGF growth factor family. VEGFA is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Alternatively spliced transcript variants, encoding either freely secreted or cell-associated isoforms, have been characterized. VEGFA is produced by a group of three major isoforms as a result of alternative splicing and if any three isoforms are produced (VEGFA120, VEGFA164, and VEGFA188) then this will not result in vessel defects and death of the full VEGFA knockout in mice.
Description:
Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three main groups of actin isoforms, α, β and γ have been identified. The α actins are found in muscle tissues and are a major constituent of the contractile apparatus. The β and γ actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, γ 1, encoded by this gene, is a cytoplasmic actin found in nonmuscle cells. FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.
Description:
Tumour necrosis factor (TNF, cachexin or cachectin and formerly known as tumour necrosis factor-alpha) is a cytokine involved in systemic inflammation and is a member of a group of cytokines that stimulate the acute phase reaction. The receptor TNF-R1 is activated by both the membrane-bound and soluble trimeric forms of TNF-alpha, whereas the receptor TNF-R2 only responds to the membrane-bound form of TNF-alpha (MultimericTNF-alpha (Prod. No. AG-40B-0019). Since the MultimericTNF-alpha mimics the membrane-bound form (forms oligomers higher than trimer), it is the only TNF-alpha protein that can activate the TNF-R2. For TNF-R1 activation, either "normal" TNF-alpha or MultimericTNF-alpha can be used."
Description:
Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. They are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpin E1 is a secreted protein which belongs to the Serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis. Defects in SERPINE1 are characterized by abnormal bleeding due to Serpin E1 defect in the plasma. High concentrations of Serpin E1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.
Description:
Increases leaving group ability of halogens; can be used for conversion of alkyl halides to triflates & acyl halides to acyl triflates; soluble in ether and other organic solvents.
Description:
Mordant orange 1 is also known as Alizarin Yellow R, C.I. 14030. Mordant orange 1 is an azo dye. Azo dyes used as biological stains contain an azo group (−N=N−). It is used for colouring many different materials such as textile, leather, and plastics and for manufacturing paints and lacquers and for printings purposes as well.
Description:
Leukemia inhibitory factor receptor is also known as LIFR; CD118; FLJ98106; FLJ99923; LIF-R; SJS2; STWS; SWS, is the receptor for leukemia inhibitory factor (LIF). The leukemia inhibitory factor is a polyfunctional cytokine that affects the differentiation, survival, and proliferation of a wide variety of cells in the adult and the embryo. LIF action appears to be mediated through a high-affinity receptor complex composed of a low-affinity LIF binding chain (LIF receptor) and a high-affinity converter subunit, gp130. Both LIFR and gp130 are members of a family of cytokine receptors that includes components of the receptors for the majority of hematopoietic cytokines and for cytokines that affect other systems, including the ciliary neurotrophic factor, growth hormone and prolactin Defects in LIFR are the cause of Stueve-Wiedemann syndrome (SWS), a severe autosomal recessive condition and belongs to the group of the bent-bone dysplasias.
UOM:
1 * 200 µG
Promotion
,PRSI96-522EA
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