| Description | Chromogenic substrate for the determination of acid and alkaline phosphatases. The reaction produces a soluble end product that is yellow in color. The reaction may be stopped with 3 N NaOH and read at 405 nm | Purity>90% SDS-PAGE.Background:Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha ) is also a component of Follicle-Stimulating Hormone (FSH), ThyroidPurity>90% SDS-PAGE.Background:Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha ) is also a component of Follicle-Stimulating Hormone (FSH), Thyroid-Stimulating Hormone, and Chorionic Gonadotropin. The unique beta subunit confers the protein’s specific biological action and is responsible for the interaction with its receptor. The approximately 20 kDa human CG alpha subunit shares 73% and 72% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively. The approximately 18 kDa human LH beta subunit shares 71% and 72% aa sequence identity with the mouse and rat orthologs, respectively. Multiple isoforms of LH exist due to differences in the post-translational glycosylation, sialylation, and sulphation modifications of its subunits. The composition, longevity, and activity of the different LH isoforms vary throughout a woman’s menstrual cycle and reproductive life cycle. LH is produced and secreted by the anterior pituitary gland. Its secretion is controlled by Gonadotropin-Releasing Hormone from the hypothalamus; however, LH secretion can also be stimulated by estradiol. LH works in concert with FSH to regulate female reproduction; FSH stimulates follicular growth and LH induces ovulation. LH also drives formation of the corpus luteum by promoting progesterone production. Additionally, LH has been suggested to stimulate the adrenal gland in postmenopausal women to induce secretion of sulfated DHEA, a precursor to androgens. In the testis, LH induces Leydig cell production of testosterone. Hypersecretion of LH has been shown to occur in women with polycystic ovary syndrome and is associated with an increased risk of infertility and miscarriage. Additionally, increased serum LH levels are associated with decreased cognition and have been implicated in the development and progression of Alzheimer’s disease. receptor into an A-frame... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes (By similarity). Acts as a transcriptional activator or repressor (By similarity). Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3' (By similarity). When overexpressed, promotes cells to enter into S phase and proliferation... Read More | Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationN-terminal Glycine.FunctionChemotactic for monocytes and T-lymphocytes. Binds to CXCR3.Post-translationalCXCL10(1-73) is produced by proteolytic cleavage after secretion from keratinocytes | 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 |