| Description | DNase I, or Deoxyribonuclease I, is an endonuclease isolated from bovine pancreas. Our DNase I Digests double str and single stranded DNA into oligo and mononucleotides.Bovine pancreatic DNase exists as four isozymes, having isoelectric points for A, B, C and D: 5.22, 4.96, 5.06 and 4.78.3. The DNase I, or Deoxyribonuclease I, is an endonuclease isolated from bovine pancreas. Our DNase I Digests double str and single stranded DNA into oligo and mononucleotides.Bovine pancreatic DNase exists as four isozymes, having isoelectric points for A, B, C and D: 5.22, 4.96, 5.06 and 4.78.3. The predominant form is A, with smaller amounts of B and C, and only minor amount of D. DNase I structure resembles the structure of to exonuclease III. It includes two central ß sheets. Each β sheet is composed of six β-strands. This complex of β sheets is surrounded by extensive loop and α-helical regions. This enzyme shares structural similarity to exonuclease III.[1]Application:Decreases viscosity providing better yields by removing DNA in primary cell isolation:Incorporating labelled bases into DNA: DNA nickRadioactive labellingBioprocessing applications: DNA removalEliminating genomic DNA from RNA preparations before RT-PCRIn vitro transcriptionNick translationDNase footprintingActin regulation of actin polymerization in cells, and cell apoptosisUV crosslinking of proteins to nucleic acidsDNase play a role in the regulation of actin polymerization in cells and is involved in apoptosis process [1]Used for the removal of DNA from protein samples... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong activator of estrogen-responsive genes. ER alpha is normally quiescent and bound to heat-shock proteins and immunophilins. Following beta -estradiol binding, it becomes activated, either homodimerizes or heterodimerizes with ER beta, and binds to DNA with multiple coactivators. Human ER alpha is 595 amino acids (aa) in length. It contains a DNA binding region (aa 185-250), three NLSs (aa 256-260; 266-271; 299-303), a steroid-binding site (aa 351-543), a dimerization motif (aa 497-518), and an O-GlcNAc attachment around Thr575. Major phosphorylation sites exist at Tyr537, Ser167 and Ser118. Multiple splice forms exist. There is an 80 kDa isoform that shows a substitution (duplication) of aa 412-517 for Asp411, a second isoform with a deletion of aa 255-366, a third isoform with a deletion of aa 152-412, and a fourth isoform that shows a Thr substitution for aa 152-595. Human ER alpha is only 46% aa identical to human ER beta. Over aa 1-116, human ER alpha shares 85% aa identity with mouse ER alpha... Read More | Purity>95% SDS-PAGE. FunctionIGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration | Purity> 95% by SDS-PAGE and HPLC analyses.FunctionSerine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect Purity> 95% by SDS-PAGE and HPLC analyses.FunctionSerine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator... 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 |