| Description | SPECIFICATIONS:Activity： GO-2 ≥100µ/mg The activity may increase up to 160% ，if Ihe reaction mixture is saturated with oxygen.Appearance： Yellow powder，lyophilizedContaminants： Catalase ≤1µ/mgStability： Stable for 24 months at 5℃SPECIFICATIONS:Activity： GO-2 ≥100µ/mg The activity may increase up to 160% ，if Ihe reaction mixture is saturated with oxygen.Appearance： Yellow powder，lyophilizedContaminants： Catalase ≤1µ/mgStability： Stable for 24 months at 5℃Additives： Sodium glutamateAPPLICATIONS :This enzyme is used for the enzymatic determination of glucosc in plasma by coupling with mutarotase，and for amylase-activity assay by coupling with α-glucosidase (if mal-tooligosaccharide or modified starch is used as a substrate) in clinical diagnosis.PACKING:Polybottle in carton-casePRESERVATION:Below 5℃ in a dry placc Fig. 5... Read More | TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification.TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin... Read More | 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： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More | Purity>98% by SDS-PAGE and HPLC analyses.FunctionAppears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic Purity>98% by SDS-PAGE and HPLC analyses.FunctionAppears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca (2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity... Read More |