| Description | Inquire | Inquire | Purity>97% SDS-PAGE and HPLC analyses. FunctionLA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen Purity>97% SDS-PAGE and HPLC analyses. FunctionLA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation.Post-translationalProteolytic removal of residues 1-9 produces the active peptide connective tissue-activating peptide III (CTAP-III) (low-affinity platelet factor IV (LA-PF4)). Proteolytic removal of residues 1-13 produces the active peptide beta-thromboglobulin, which is released from platelets along with platelet factor 4 and platelet-derived growth factor. NAP-2(1-66) is produced by proteolytical processing, probably after secretion by leukocytes other than neutrophils. NAP-2(73) and NAP-2(74) seem not be produced by proteolytical processing of secreted precursors but are released in an active form from platelets... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:The HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C)expressed in and purified from Escherichia coli. HRV 3C Protease cleaves protein substrates with the recognition Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:The HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C)expressed in and purified from Escherichia coli. HRV 3C Protease cleaves protein substrates with the recognition sequence Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro between the Gln and Gly residues. The high specificity and affinity tags( 6xHis) of the protease make it an ideal choice for the removal of purification and detection tags on recombinant proteins and allows for flexibility in protease removal.Source:HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C) expressed in and purified from Escherichia coli.HRV 3C enzyme digestion of His-GST-IL33 protein, according to the mass ratio (HRV 3C: target protein) 1:25 and 1:50 enzyme digestion, overnight at 4℃ enzyme digestion results are as follows: completely clean enzyme digestion... Read More | Purity≥95% SDS-PAGE.Endotoxin level<0.1 EU/µgFunctionInhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate Purity≥95% SDS-PAGE.Endotoxin level<0.1 EU/µgFunctionInhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma.Post-translationalO-glycosylated... Read More |