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100g Pack Size. Group: Biochemicals, Diagnostic Raw Materials. Formula: N/A. CAS No. 9013-90-5. Prepack ID 10760053-100g. See USA prepack pricing.
Lactalbumin
500g Pack Size. Group: Biochemicals, Diagnostic Raw Materials. Formula: N/A. CAS No. 9013-90-5. Prepack ID 10760053-500g. See USA prepack pricing.
LACTALBUMIN
Heterocyclic Organic Compound. Alternative Names: EC 2.4.1.22;LACTALBUMIN;ALBUMIN (MILK);ALBUMIN LACTIC;ALPHA-LACTALBUMIN. CAS No. 12585-12-5. Purity: N/A. Catalog: ACM12585125.
α-Lactalbumin
α-Lactalbumin is a Ca 2+ -binding protein. α-Lactalbumin has a single strong Ca 2+ -binding site and for this reason it frequently serves as a simple model Ca 2+ -binding protein. α-Lactalbumin is a component of lactose synthase, an enzyme system, which consists of galactosyltransferase (GT) and α-Lactalbumin [1] [2]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 9051-29-0. Pack Sizes: 5 mg; 10 mg. Product ID: HY-NP009.
Cortisol 21-Mesylate
Cortisol (H714615) derivative. A glucocorticoid that augments the accumulation of α-lactalbumin in midpregnant rat mammary tissue cultured in the presence of insulin and prolactin. Group: Biochemicals. Alternative Names: Hydrocortisone 21-Mesylate; 11,17-Dihydroxy-21-[(methylsulfonyl)oxy]-pregn-4-ene-3,20-dione. Grades: Highly Purified. CAS No. 6677-96-9. Pack Sizes: 250mg. US Biological Life Sciences.
Worldwide
lactose synthase
The enzyme is a complex of two proteins, A and B. In the absence of the B protein (α-lactalbumin), the enzyme catalyses the transfer of galactose from UDP-α-D-galactose to N-acetylglucosamine (EC 2.4.1.90 N-acetyllactosamine synthase). Group: Enzymes. Synonyms: UDP-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase. Enzyme Commission Number: EC 2.4.1.22. CAS No. 9030-11-9. Galactosyltransferase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2448; lactose synthase; EC 2.4.1.22; 9030-11-9; UDP-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase. Cat No: EXWM-2448.
Lysozyme 23A from Bacillus subtilis, Recombinant
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequ... lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Purity: >90% by SDS-PAGE. Lysozyme. Mole weight: 20.5 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus subtilis. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2; Lysozyme 23A. Cat No: NATE-1455.
Lysozyme 25A from Streptococcus pneumoniae, Recombinant
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in ... LYZ; LZM; EC 3.2.1.17; 9001-63-2. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Purity: >90% by SDS-PAGE. Lysozyme. Mole weight: 26.3 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Streptococcus pneumoniae. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2; Lysozyme 25A. Cat No: NATE-1456.
Lysozyme from Human, Recombinant
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene. Group: Enzymes. Synonyms: muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Lysozyme. Activity: > 100 ,000 units/mg protein (E1%/280). Storage: -70°C. Form: lyophilized powder. Source: Rice. Species: Human. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Pack: Package size based on protein content. Cat No: NATE-0434.
Native Bovine Galactosyltransferase
Galactosyltransferase catalyzes the transfer of galactosyl molecules in the synthesis of oligosaccharides. Applications: Galactosyltransferase is the catalytic component of the lactose synthetase system; it synthesizes lactose slowly in the absence of the regulatory protein α-lactalbumin. galactosyltransferase will also transfer galactose from udp-galactose to n-acetylglucosamine. this preparation is useful in the determination of α-lactalbumin, udp-galactose, and n-acetylglucosamine. Group: Enzymes. Synonyms: EC 2.4.1.22; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; 9031-68-9. Enzyme Commission Number: EC 2.4.1.22. CAS No. 9031-68-9. Galactosyltransferase. Storage: -20°C. Form: Lyophilized powder containing Tris, EDTA, and (NH4)2SO4. Source: Bovine milk. Species: Bovine. EC 2.4.1.22; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; 9031-68-9. Cat No: NATE-0274.
Native Bovine Trypsin
Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the remova...te is dependent primarily on the cell type and the age of the culture. trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps. trypsin can be used to release adherent cells from tissue culture plates for passaging. trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. trypsin has also been use
Native Chicken Lysozyme chloride form
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence ...lmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Lysozyme. Mole weight: mol wt ~14.3 kDa. Activity: > 100,000 units/mg protein (E1%/280). Storage: -20°C. Form: Lyophilized powder containing sodium chloride and sodium acetate. Source: Chicken egg white. Species: Chicken. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Cat No: NATE-0432.
Native Human Lysozyme
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene. Group: Enzymes. Synonyms: muramidase; globulin G; mucopeptide gl. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Purity: > 95% (SDS-PAGE). Lysozyme. Activity: > 100 ,000 units/mg protein (E1%/280). Storage: -20°C. Form: Lyophilized from 50 mM sodium acetate, pH 6.0, with 100 mM NaCl. Source: Human neutrophils. Species: Human. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Cat No: NATE-0433.
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