| 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 | Inquire | Recombinant human basic fibroblast growth factor (also known as basic FGF, bFGF, FGF2, FGF-beta, or heparin-binding growth factor), is a biologically active protein suitable for cell culture applications. bFGF regulates diverse processes such as cell proliferation, differentiation, survival, Recombinant human basic fibroblast growth factor (also known as basic FGF, bFGF, FGF2, FGF-beta, or heparin-binding growth factor), is a biologically active protein suitable for cell culture applications. bFGF regulates diverse processes such as cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation, and wound recovery. bFGF can be used in studies of angiogenesis, fibroblast mitosis, axonal outgrowth in PC-12 cells, receptor binding, and tyrosine phosphorylation. This strain is expressed in recombinant Escherichia coli, and after multi-step separation and purification, it is dissolved in 10mM PBS, 0.15 M NaCl (pH7.2) solution, filtered through a 0.22 µm filter membrane, and then freeze-dried to make a lyophilized powder... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:ROR1 (Receptor tyrosine kinase-like orphan receptor 1), also known as neurotrophic tyrosine kinase receptor-related 1 (NTRKR1), is a member of the ROR family within the receptor tyrosine kinases (RTK) superfamily. Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:ROR1 (Receptor tyrosine kinase-like orphan receptor 1), also known as neurotrophic tyrosine kinase receptor-related 1 (NTRKR1), is a member of the ROR family within the receptor tyrosine kinases (RTK) superfamily. Two ROR family members (ROR1 and ROR2) have been identified and are characterized by their intracellular tyrosine kinase domains, which are highly related to those of the Trk-family receptor tyrosine kinases, and by their extracellular Frizzled-like cysteine-rich domains and kringle domains, common to receptors of the Wnt family members. Human ROR1 is a type I transmembrane protein with 937 amino acids in length. It contains a 29 amino acid signal sequence, a 377 amino acid extracellular domain (ECD), a 21 amino acid transmembrane segment, and a 510 amino acid cytoplasmic region. Human ROR1 shares 97% and 58% amino acid sequence identity with mouse ROR1 and human ROR2, respectively. ROR1 has been shown to play crucial roles in developmental morphogenesis by acting as receptors or co-receptors to mediate Wnt5a-induced signaling. The bioactivity of ROR1 is measured by its ability to bind biotinylated recombinant mouse Wnt-5a in a functional ELISA... Read More | Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane It is required for normal Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane It is required for normal hematopoietic function and plays an important role in hematopoiesis, spermatogenesis, and melanogenesis. It also promotes mast cell adhesion, migration, proliferation, and survival. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. Recombinant murine SCF is an 18.4kDa polypeptide containing 165 amino acid residues.Purity＞97% (SDS-PAGE,HPLC)FunctionLigand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.Post-translationalA soluble form (sKITLG) is produced by proteolytic processing of isoform 1 in the extracellular domain. Found in two differentially glycosylated forms, LMW-SCF and HMW-SCF. LMW-SCF is fully N-glycosylated at Asn-145, partially N-glycosylated at Asn-90, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97 or Asn-118. HMW-SCF is N-glycosylated at Asn-118, Asn-90 and Asn-145, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97. A soluble form exists as a cleavage product of the extracellular domain... Read More |