| Description | α-Amylase belongs to glycosyl hydrolase family 13. It comprises of A, B and C domains. Domain A has two aspartic acid and a glutamic acid as catalytic residues. Domain B possesses Ca2+ and Na+ binding sites.Application:α-Amylase from Bacillus sp. has been used in the digestion of α-Amylase belongs to glycosyl hydrolase family 13. It comprises of A, B and C domains. Domain A has two aspartic acid and a glutamic acid as catalytic residues. Domain B possesses Ca2+ and Na+ binding sites.Application:α-Amylase from Bacillus sp. has been used in the digestion of lyophilized microalgae sample. It has also been used to evaluate α-amylase inhibitory activity in marine algae samples and Myrmecodia platytyrea... Read More | Inquire | Inquire | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg2+-dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg2+-dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the glycolytic pathway and catalyzes the reverse reaction in gluconeogenesis. There are three major isozymes of enolase expressed in selective vertebrate tissues from separate genes: alpha (ENO1), beta (ENO3), and gamma (ENO2). NSE is a highly expressed, specific neuron isozyme making it a useful marker for tumors derived from neuronal cells. Neuron-specific enolase is implicated as a diagnostic and prognostic marker in numerous diseases including early small cell lung cancer, prostate cancer, multiple myeloma, traumatic brain injury, acute spinal cord injury, acute ischemic stroke, and post-concussion symptoms. NSE expression and activity are increased in neuronal and glial activation and injury, risk factors implicated in neurodegenerative disease. Elevation of NSE promotes glycolysis, proliferation, activation and migration through its C-terminus to activate PI3K and MAPK signal transduction pathways while inhibition of enolase has been shown to attenuate inflammatory events. NSE can be regulated through cleavage of the C-termini by cathepsin X or inhibited directly by antibiotic SF2312. Inhibition has been proposed as a therapeutic strategy in cancer... Read More | Background：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisitsBackground：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 179 aa extracellular domain (ECD). Within the ECD, rat TNF-alpha shares 94% aa sequence identity with mouse and 69%-76% with bovine, canine, cotton rat, equine, feline, human, porcine, and rhesus TNF-alpha. TNF-alpha is produced by a wide variety of immune, epithelial, endothelial, and tumor cells. TNF-alpha is assembled intracellularly to form a noncovalently linked homotrimer which is expressed on the cell surface. Cell surface TNF-alpha can induce the lysis of neighboring tumor cells and virus infected cells, and it can generate its own downstream cell signaling following ligation by soluble TNFR I. Shedding of membrane bound TNF-alpha by TACE/ADAM17 releases the bioactive cytokine, a 55 kDa soluble trimer of the TNF-alpha extracellular domain. TNF-alpha binds the ubiquitous 55-60 kDa TNF RI and the hematopoietic cell-restricted 80 kDa TNF RII, both of which are also expressed as homotrimers. Both type I and type II receptors bind TNF-alpha with comparable affinity, although only TNF RI contains a cytoplasmic death domain which triggers the activation of apoptosis. Soluble forms of both types of receptors are released and can neutralize the biological activity of TNF-alpha. Post-translational modificationsThe soluble form derives from the membrane form by proteolytic processing.The membrane form, but not the soluble form, is phosphorylated on serine residues.Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid... Read More |