| Description | The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.PROPERTIESMolecular weight: ca. 34 kDa (gel filtration)Structure: monomer of ca. 25 kDa (SDS-PAGE)Michaelis constant: 2.3×10^−4 M (β-d-glucose-1-phosphate)pH Optimum: ca. 7.0 (The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.PROPERTIESMolecular weight: ca. 34 kDa (gel filtration)Structure: monomer of ca. 25 kDa (SDS-PAGE)Michaelis constant: 2.3×10^−4 M (β-d-glucose-1-phosphate)pH Optimum: ca. 7.0 (Fig. 1)pH Stability: 5.0–9.5 (Fig. 2)Optimum temperature: 40°C (Fig. 3)Thermal stability: below 45°C (Fig. 4)Stability (liquid form): stable at 37°C for at least one week (Fig. 5)Stability (powder form): stable at 30°C for at lest one month (Fig. 6)Activators: Mg2+, Mn2+, Co2+, Ni2+Inhibitors: Hg2+, Zn2+, Cu2+, Cd2+STABILIZERS: lactose, EDTAASSAY PROCEDURE PrincipleThe appearance of NADPH is measured spectrophotometrically at 340 nm.ReagentsA. HEPES–NaOH buffer, 0.3 M; pH 7.0, containing 40 mM KCl, 4 mM MgCl2 and 1.6% (w/v) Triton X-100: dissolve 7.15 g of HEPES, 298 mg of KCl, 81.3 mg of MgCl2·6H2O and 1.6 g of Triton X-100 in 75 ml of distilled water, adjust to pH 7.0 with 4 N NaOH and dilute with distilled water to 100 ml.B. d-Glucose-1,6-bisphosphate (G-1,6-P2) solution, 3.0 mM : 60.7 mg of G-1,6-P2 cyclohexylammonium·4H2O/ 25 ml of distilled water.C. NADP+ solution, 12 mM: 230 mg of NADP+·Na/25 ml of distilled water.D. β-d-Glucose-1-phosphate (β-G-1-P) solution, 22 mM:167 mg of β-G-1-P disodium salt/25 ml of distilled water.E. Glucose-6-phosphate dehydrogenase (G6PDH) solution: 1750 U/ml.F. Enzyme dilution buffer: mix 10 mM KH2PO4 solution and 10 mM K2HPO4 solution to make a pH 7.0 solution.Sample: dissolve the lyophilized enzyme to a volume activity of 1.0–3.0 U/ml with ice-cold enzyme dilution buffer (Reagent F) immediately before measurement. Procedure1. Pipette the following reagents into a cuvette (light path: 1 cm).1.5 ml HEPES–NaOH buffer (Reagent A)0.3 ml G-1,6-P2 solution (Reagent B)0.3 ml NADP+ solution (Reagent C)0.3 ml β-G-1-P solution (Reagent D) 0.02 ml G6PDH solution (Reagent E)0.6 ml Distilled water2. Equilibrate at 37°C for about 5 min.3. Add 0.03 ml of sample and mix.4. Record the increase of absorbance at 340 nm in a spectrophotometer thermostated at 37°C, and calculate the ∆Aper min using the linear portion of the curve (∆AS).The blank solution is prepared by adding enzyme dilution buffer (Reagent F) instead of sample (∆A0).CalculationActivity can be calculated by using the following formula:6.2: Millimolar extinction coefficient of NADPH at 340 nm (cm2/µmol)df: Dilution factorC: Content of β-phosphoglucomutase preparation in sample (mg/ml)APPLICATIONSThe enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.EXPERIMENTAL DATA... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Binds electronegative LDL (LDL-) and mediates the cytokine release induced by LDL-... Read More | Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.Background:Human HB-EGF (Heparin-Binding EGF-like growth factor) is a 12-16 kDa member of the EGF family of peptide growth factors (1-3). Also known as the DTR (diphtheria toxin receptor), it is further classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors (4, 5). HB-EGF is synthesized as a 208 amino acid (aa) type I transmembrane preproprecursor (1, 6). It contains a 19 aa signal sequence, a 43 aa prosegment, an 86 aa mature region (aa 63-148), an 11 aa juxtamembrane cleavage peptide, a 24 aa transmembrane segment, and a 25 aa cytoplasmic tail (aa 184-208). As an integral membrane protein, HB-EGF is expressed as a 19-27 kDa protein in mammalian cells (7-9). The variability in molecular weight (MW) is attributed to heterogeneity in glycosylation and/or the utilization of multiple proteolytic cleavage sites during maturation. Mature HB-EGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. It possesses an EGF-like domain between aa 104-144, and a heparin-binding motif between aa 93‑113. Although the aa range for "mature" HB-EGF is typically stated to be Asp63-Leu148, potential N-terminal start (cleavage) sites also exist at Gly32, Arg73, Val74, Ser77 and Ala82 (8, 10-12). Thus, differential processing (in part) likely accounts for the 16-23 kDa range in MW noted for mammalian-derived mature HB-EGF. Proteases suggested to contribute to HB-EGF processing include TACE, MMP-3 and -7, ADAM-17 and ADAM-12 (11, 13-16). When expressed recombinantly in E.coli, HB-EGF (aa 73-148) runs at 14 kDa in SDS-PAGE; when expressed in Baculovirus, HB-EGF (aa 63-148, 77-148 and 32-148) runs at 18 kDa, 15 kDa, and 19 kDa respectively (8, 12, 17). Over aa 63-148, human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF, respectively (1, 18). Cells known to express HB-EGF include bronchial epithelium (19), visceral and vascular smooth muscle (20, 21), CD4+ T cells (22), cardiac muscle (23), glomerular podocytes (24), keratinocytes (13) and IL-10-secreting regulatory macrophages (25). As noted earlier, HB-EGF is known to bind to both 170 kDa EGFR and 180 kDa ErbB4, and through heterodimerization, ErbB2 (13, 26). Activity associated with ErbB4 binding appears to be limited to non-mitogenic actions, while EGFR binding induces both mitogenic and non-mitogenic activity... 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:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：The monkeypox virus is the causative agent of the infectious disease of monkeypox. The virus is a member of the Orthopoxvirus genus in the family Poxviridae. And its genome is a double-stranded DNA. The Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：The monkeypox virus is the causative agent of the infectious disease of monkeypox. The virus is a member of the Orthopoxvirus genus in the family Poxviridae. And its genome is a double-stranded DNA. The disease caused by the virus is similar to but milder than smallpox and its mortality is often much lower. Humans and animals are both hosts for monkeypox virus and both species are vulnerable to the virus and may develop diseases. Monkeypox virus is mainly distributed in rainforests of west and central Africa. Isolates from Central Africa and Western Africa is different in virulence and the former is more virulent than the latter. The virus could spread in animals and humans and direct contact with the body fluid of an infected animal or being bitten may infect the virus... Read More |