| Description | COX6B2 Human Pre-designed siRNA Set A contains three designed siRNAs for COX6B2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components COX6B2 siRNA-1: 5 nmol (HPLC) COX6B2 siRNA-2: 5 nmol (HPLC) COX6B2 siRNA-3: 5 nmol (HPLC) siRNA Negative COX6B2 Human Pre-designed siRNA Set A contains three designed siRNAs for COX6B2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components COX6B2 siRNA-1: 5 nmol (HPLC) COX6B2 siRNA-2: 5 nmol (HPLC) COX6B2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.Animal origin free:eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B.Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease activities found in extracted enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 3）Less than 10ppm of recombinant trypsin... Read More | 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 | Product IntroductionHuman epidermal growth factor (EGF) has a molecular weight of 6 KD, contains 53 amino acids, and has three intramolecular disulfide bonds.Upon binding to EGFR, a specific receptor located on the cell surface, EGF causes a series of biochemical reactions in the cell: increasing Product IntroductionHuman epidermal growth factor (EGF) has a molecular weight of 6 KD, contains 53 amino acids, and has three intramolecular disulfide bonds.Upon binding to EGFR, a specific receptor located on the cell surface, EGF causes a series of biochemical reactions in the cell: increasing the level of calcium ion concentration in the cell, promoting the progress of glycolysis, increasing the synthesis of proteins, and can enhance the expression of EGFR, a specific class of genes to promote DNA synthesis and cell proliferation.Specification parametersSource Pichia pastorisAppearance white lyophilized powderActivity ≥1.0×106IU/mgpH 6.5-7.5Molecular weight 6.5kDEndotoxin ≦1.0 EU/mgCAS No 62253-63-8Matters needing attentionReconstitution: reconstitution of REGF lyophilized powder to 100-200 µg/ml with sterile water is recommended and further dilution with other solvents may be performed.REGF dissolved at 4 ° C can be stored for 2-7 days and used up as soon as possible.To not use for short periods, store at - 20 ℃.Use as soon as possible after opening to avoid contamination.Limitations of useIt is suitable for research, laboratory and production use only and cannot be used directly in humans... Read More | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. The mechanism of HMOX is unique in that heme serves as the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HMOX activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HMOX1 and HMOX2, are expressed in most tissues. HMOX1 is an inducible enzyme in response to heme, heavy metals, oxidative stress, cytokines, and many drugs. Whereas HMOX2 displays a constitutive expression. HMOX1 is expressed mainly in spleen, liver, and kidney, and HMOX2 is prominently expressed in the brain and testes. The increased expression of HMOX1 levels is related to a variety of pathological states, where it functions as a cytoprotective molecule through its by products. HMOX1 also plays important roles in the regulation of cell proliferation, differentiation, and apoptosis... Read More |