United States Biological Corporation ANTI-HEPARAN SULFATE DELTA DFS Item

NC0219556 Heparan sulfate, otherwise known as heparitin sulfate or heparin monosulfate, is a generic term describing polysaccharides which are linear and consist of N-acetylated [->4)alpha-D-GlcNpAc-(1->4) �-D-GlcAp(1->] and N-sulfated disaccharides [->4)alpha-D-GlcNpS- (1->4)-�-D-GlcAp or alpha-L-IdoAp(1->] that are arranged mainly in a segregated manner. The sulfate-rich fractions in heparan sulfate are heparin-like, though they rarely possess the sulfate density found in heparin. Approximately 25% of the total polymer is initially formed by alternating arrangements of the two disaccharide units, ->4)alpha-D-GlcNpS(1->4)UAp(1->4) alpha-D-GlcNpAc(1->4)UAp (1->4)-alpha-D-GlcAp(1->. The polymer is formed as a repeating ->4)-alpha-D-GlcNpAc (1->4)-�-D-GlcAp(1-> disaccharide sequence that is attached to a serine residue of a core protein through a tetrasaccharide, glucuronosyl->galactosyl->galactosyl->xylosyl, linkage region. Heparan sulfate, otherwise known as heparitin sulfate or heparin monosulfate, is a generic term describing polysaccharides which are linear and consist of N-acetylated [->4)alpha-D-GlcNpAc-(1->4) �-D-GlcAp(1->] and N-sulfated disaccharides [->4)alpha-D-GlcNpS- (1->4)-�-D-GlcAp or alpha-L-IdoAp(1->] that are arranged mainly in a segregated manner. The sulfate-rich fractions in heparan sulfate are heparin-like, though they rarely possess the sulfate density found in heparin. Approximately 25% of the total polymer is initially formed by alternating arrangements of the two disaccharide units, ->4)alpha-D-GlcNpS(1->4)UAp(1->4) alpha-D-GlcNpAc(1->4)UAp (1->4)-alpha-D-GlcAp(1->. The polymer is formed as a repeating ->4)-alpha-D-GlcNpAc (1->4)-�-D-GlcAp(1-> disaccharide sequence that is attached to a serine residue of a core protein through a tetrasaccharide, glucuronosyl->galactosyl->galactosyl->xylosyl, linkage region.

United States Biological Corporation ANTI-GLYCERALDEHYDE-3PHOSPHATE DFS Item

NC0356794 Glyceraldehyde 3-Phosphate Dehydrogenase (GAPD, GAPDH) (Glycerol Free) Mab Mo xRb E B IC IF Glyceraldehyde 3-Phosphate Dehydrogenase (GAPD, GAPDH) (Glycerol Free) Mab Mo xRb E B IC IF

United States Biological Corporation RABBIT ANTI-PHOSPHO-AXL (Y691) DFS Item

NC1118329 Rabbit Anti-Phospho-Axl (Y691) Rabbit Anti-Phospho-Axl (Y691)

United States Biological Corporation 1 LITER OF 30% BSA DFS Item

NC0424588 A highly purified, liquid form of albumin suitable for ELISA systems, as an enzyme or protein stabilization agent, as a blocking agent to prevent non-specific protein binding, Rh-typing sera diluents, crossmatching procedures, and for molecular biology procedures where low IgG and protease background levels are required. Albumin is sterile-filtered using a 0.2um filter. Percent Albumin: 30-31% Albumin Purity (HPLC): ≥98.0% Appearance: 0.22um filtered pale-green to amber, clear solution Protease: ≤1ug/ml IgG: None detected Microbial Growth: ≤3 cfu/ml Vesicular Stomatitis Virus: Negative Bluetongue Virus: Negative pH (3%): 6.9-7.3 Conductivity (3%): ≤3000uS/cm (umhos/cm) Sodium (3%): ≤80meq/L Chloride (3%): ≤50meq/L Calcium (3%): ≤2.5mg/dL Iron (3%): ≤110ug/dL Free Fatty Acids: ≤0.01% A highly purified, liquid form of albumin suitable for ELISA systems, as an enzyme or protein stabilization agent, as a blocking agent to prevent non-specific protein binding, Rh-typing sera diluents, crossmatching procedures, and for molecular biology procedures where low IgG and protease background levels are required. Albumin is sterile-filtered using a 0.2um filter. Percent Albumin: 30-31% Albumin Purity (HPLC): ≥98.0% Appearance: 0.22um filtered pale-green to amber, clear solution Protease: ≤1ug/ml IgG: None detected Microbial Growth: ≤3 cfu/ml Vesicular Stomatitis Virus: Negative Bluetongue Virus: Negative pH (3%): 6.9-7.3 Conductivity (3%): ≤3000uS/cm (umhos/cm) Sodium (3%): ≤80meq/L Chloride (3%): ≤50meq/L Calcium (3%): ≤2.5mg/dL Iron (3%): ≤110ug/dL Free Fatty Acids: ≤0.01%

United States Biological Corporation TRIS HCL BUFFER 1M PH7.5500ML DFS Item

NC0735932 Tris is one of the most widely used buffers in molecular biology and cell culture due to its low toxicity, stability and buffering capacity. Purity: ≥99.9% Appearance: White, crystalline powder pH (1M): 10.5-11.5 pKa: 8.0-8.4 Absorbance (260nm): ≤0.06 Absorbance (280nm): ≤0.05 Absorbance (290nm): ≤0.2 Solubility (1M): Colorless, clear, complete Loss on Drying: ≤0.2% Melting Point: 168-172°C Heavy Metals (Pb): ≤0.0001% Arsenic: ≤0.0001% Calcium: ≤0.0001% Copper: ≤0.0001% Iron: ≤0.0005% Magnesium: ≤0.0001% Insoluble Matter: ≤0.005% Residue on Ignition: ≤0.1% RNase: DNase: Protease: Meets specifications. Tris is one of the most widely used buffers in molecular biology and cell culture due to its low toxicity, stability and buffering capacity. Purity: ≥99.9% Appearance: White, crystalline powder pH (1M): 10.5-11.5 pKa: 8.0-8.4 Absorbance (260nm): ≤0.06 Absorbance (280nm): ≤0.05 Absorbance (290nm): ≤0.2 Solubility (1M): Colorless, clear, complete Loss on Drying: ≤0.2% Melting Point: 168-172°C Heavy Metals (Pb): ≤0.0001% Arsenic: ≤0.0001% Calcium: ≤0.0001% Copper: ≤0.0001% Iron: ≤0.0005% Magnesium: ≤0.0001% Insoluble Matter: ≤0.005% Residue on Ignition: ≤0.1% RNase: DNase: Protease: Meets specifications.

United States Biological Corporation X/GAL 40MG PER ML/DMF 10ML EA DFS Item

NC9231777 Blue substrate used in the detection of b-galactosidase in bacteria or phage as a selection agent for cloning experiments utilizing the lacZ vector. Colonies expressing b-galactosidase will appear blue in the presence of XGAL. Others will appear white. Gene Cloning: In gene cloning, X-gal is used as a visual indication of whether a cell expresses a functional ²-galactosidase enzyme in a technique called blue/white screening. This method of screening is a convenient way of distinguishing a successful cloning product from other unsuccessful ones. The blue/white screening method relies on the principle of ±-complementation of the ²-galactosidase gene, where a fragment of the lacZ gene (lacZ±) in the plasmid can complement another mutant lacZ gene (lacZ”M15) in the cell. Both genes by themselves produce non-functional peptides, however, when expressed together, as when a plasmid containing lacZ± is transformed into a lacZ”M15 cells, they form a functional ²-galactosidase. Blue substrate used in the detection of b-galactosidase in bacteria or phage as a selection agent for cloning experiments utilizing the lacZ vector. Colonies expressing b-galactosidase will appear blue in the presence of XGAL. Others will appear white. Gene Cloning: In gene cloning, X-gal is used as a visual indication of whether a cell expresses a functional ²-galactosidase enzyme in a technique called blue/white screening. This method of screening is a convenient way of distinguishing a successful cloning product from other unsuccessful ones. The blue/white screening method relies on the principle of ±-complementation of the ²-galactosidase gene, where a fragment of the lacZ gene (lacZ±) in the plasmid can complement another mutant lacZ gene (lacZ”M15) in the cell. Both genes by themselves produce non-functional peptides, however, when expressed together, as when a plasmid containing lacZ± is transformed into a lacZ”M15 cells, they form a functional ²-galactosidase.

United States Biological Corporation ZYMOLYASE 20T DFS Item

NC0236652 Zymolyase, produced by a submerged culture of Arthrobacter luteus (1), is an enzyme preparation which effectively lyses cell walls of viable yeast cells. An essential enzyme responsible for lysis of viable yeast cells in this preparation is b-1, 3-glucan laminaripentaohydrolase. It hydrolyzes linear glucose polymers with b-1,3-linkages and releases laminaripentaose specifically as the main and minimum product unit (4,5,10,11). This lytic activity releases spheroplasts and protoplasts in the preparation of yeast DNA prior to restriction enzyme digestion and Southern Blot analysis. The extent of lysis of yeast cells by Zymolyase varies with yeast strain, growth stage of yeast and cultural condition (6-8). Further information related to Zymolyase is obtained in the references below. Source: Arthrobactor luteus Applications: Protoplast/Spheroplast Preparation Yeast Cell Fusion Yeast Cell Transformation Appearance: Lyophilized powder Activity: 20u/mg Zymolyase, produced by a submerged culture of Arthrobacter luteus (1), is an enzyme preparation which effectively lyses cell walls of viable yeast cells. An essential enzyme responsible for lysis of viable yeast cells in this preparation is b-1, 3-glucan laminaripentaohydrolase. It hydrolyzes linear glucose polymers with b-1,3-linkages and releases laminaripentaose specifically as the main and minimum product unit (4,5,10,11). This lytic activity releases spheroplasts and protoplasts in the preparation of yeast DNA prior to restriction enzyme digestion and Southern Blot analysis. The extent of lysis of yeast cells by Zymolyase varies with yeast strain, growth stage of yeast and cultural condition (6-8). Further information related to Zymolyase is obtained in the references below. Source: Arthrobactor luteus Applications: Protoplast/Spheroplast Preparation Yeast Cell Fusion Yeast Cell Transformation Appearance: Lyophilized powder Activity: 20u/mg

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