| Description | DescriptionBovine Serum Albumin (BSA) is a high purity, lyophilized "Fraction V" powder derived from the plasma of MPI-inspected healthy New Zealand origin animals. The albumin is isolated from other plasma protein products and lipids by a unique proprietary, non-solvent procedure. The separation DescriptionBovine Serum Albumin (BSA) is a high purity, lyophilized "Fraction V" powder derived from the plasma of MPI-inspected healthy New Zealand origin animals. The albumin is isolated from other plasma protein products and lipids by a unique proprietary, non-solvent procedure. The separation process includes a modified Cohn / heat-shock procedure designed to inactivate proteases and other potentially interfering enzymes. Further processing such as extensive membrane dialysis and filtration, minimizes analytes that can cause background interference in sensitive in vitro diagnostic (IVD) assays as well as inhibition in sensitive cell and microbial culture systems. Typical purity levels are in excess of 99%. New Zealand Source Standard Grade bovine albumin product is an economical choice that is ideal for most diagnostic and research applications.ApplicationsProtease-sensitive Immunoassays such as RIA, EIA, Fluorescent and ChemiluminescentProtein Standard, DiluentProtein, Conjugate or Enzyme StabilizerHybridizationSelected Cell Culture applicationsFeatures/BenefitsHigh Purity, Low Interference, Low BackgroundVirtually No Detectable Protease Activity, Ensures Assay Integrity“Closed Loop” Manufacturing* – Minimizes Contamination and Maximizes ReproducibilitySuperior Solubility/Filterability for Ease of UseProduct Development and Technical Services Designed for maximum responsiveness and FlexibilityManufactured from MPI inspected Bovine PlasmaManufactured According to FDA cGMPsValidated for Prion (TSE) ClearanceSpecificationsProtein (dry basis) ≥ 96.0%Purity (albumin) ≥ 98%Solubility (4% water) Clear/slightly hazyMoisture ≤ 5.0%pH (10% water) 6.5 to 7.5Ash < 2%Protease ≤ 0.005 Units/mgEndotoxin ≤ 3 EU/mgIgG Not DetectedPhysical CharacteristicsBovine Serum Albumin is a highly soluble yellow to green with tan to green cast lyophilized powder. A solution of up to 30% in de-ionized water is clear to slightly hazy and virtually particulate-free.Storag RecommendationsStore sealed in a cool, dry environment for 3 years, and up to 5 years with re-qualification... Read More | Inquire | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong activator of estrogen-responsive genes. ER alpha is normally quiescent and bound to heat-shock proteins and immunophilins. Following beta -estradiol binding, it becomes activated, either homodimerizes or heterodimerizes with ER beta, and binds to DNA with multiple coactivators. Human ER alpha is 595 amino acids (aa) in length. It contains a DNA binding region (aa 185-250), three NLSs (aa 256-260; 266-271; 299-303), a steroid-binding site (aa 351-543), a dimerization motif (aa 497-518), and an O-GlcNAc attachment around Thr575. Major phosphorylation sites exist at Tyr537, Ser167 and Ser118. Multiple splice forms exist. There is an 80 kDa isoform that shows a substitution (duplication) of aa 412-517 for Asp411, a second isoform with a deletion of aa 255-366, a third isoform with a deletion of aa 152-412, and a fourth isoform that shows a Thr substitution for aa 152-595. Human ER alpha is only 46% aa identical to human ER beta. Over aa 1-116, human ER alpha shares 85% aa identity with mouse ER alpha... Read More | 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 |