| Description | Collagen ll-binding peptide is a polypeptide product in the form of TFA salt | Inquire | description：Bovine pancreatic deoxyribonuclease I produced recombinantly in yeast, Pichia pastoris, to decrease levels of contaminating RNase and eliminate potential pathogens associated with animal based materials.Bovine pancreas is a rich source of RNase A which is often found in many description：Bovine pancreatic deoxyribonuclease I produced recombinantly in yeast, Pichia pastoris, to decrease levels of contaminating RNase and eliminate potential pathogens associated with animal based materials.Bovine pancreas is a rich source of RNase A which is often found in many commercial DNase preparations. Producing DNase I by recombinant means in an organism with much lower levels of endogenous RNase greatly facilitates purification of an enzyme with undetectable levels of RNase. The processes involved in the production and isolation of recombinant DNase I are completely devoid of animal based components which eliminates the possibility of introducing animal derived pathogens into bioprocessing procedures.Animal Free/AF. Recombinant Bovine pancreatic deoxyribonuclease 1 produced in Pichia pastoris. Chromatographically purified. Free of animal derived components, RNases & proteases. A liquid preparation in 5mM Calcium Acetate, 4mg/ml glycine, pH 5.0 and 50% glycerol. Supplied with 10x reaction buffer.Storage Buffer : 5mM calcium acetate, 4mg/ml glycine, pH 5.0 and 50% glycerol.DNase I Reaction Buffer (10X): 500mM Tris-HCl, 10mM MgSO4, 1mM CaCl2, pH 7.8, provided.application：Recombinant DNase I is suitable for such applications as:• Removing genomic DNA from RNA preparations prior to RT-PCR• Degradation of DNA templates after transcription reactions• Removing unwanted DNA from samples prior to Northern blotting• Removing DNA during biopharma and bioprocessing procedures... Read More | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa precursor protein that is cleaved at a dibasic proteolytic site into a 40 kDa membrane-bound protein termed MSLN and a 31 kDa shed fragment called megakaryocyte-potentiating factor (MPF) that is released from the cell. Cleaved, human MSLN remains attached to the cell surface via a GPI linkage and shares 58% amino acid sequence identity with mouse and rat MSLN. In human, alternate splicing generates additional MSLN isoforms that have either an eight amino acid insertion following Ser408 or a substituted C‑terminal region with no GPI anchor. Mesothelin is normally expressed on mesothelial cells in the pleura, pericardium, and peritoneum as well as in the developing and postnatal pancreas. It is up‑regulated in mesotheliomas and a range of carcinomas and adenomas. Mesothelin promotes tumor cell proliferation, migration, anchorage-independent growth, and tumor progression. It is co‑expressed with the tumor antigen CA125/MUC16 on advanced ovarian adenocarcinomas and interacts with this molecule to support cell adhesion. A soluble form of Mesothelin is released from tumor cells into the serum or tissue effusions... Read More | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More |