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(5-Bromo-4-chloro-3-indolyl Phosphate/Nitroblue Tetrazolium)Stabilized Chromogen SolutionSpecially prepared for immunoblotting procedures only. Concentration: 0.577 mmol/liter BCIP; 0.122 mmol/liter NBT.
BCIP/NBT Liquid Substrate Plus is a stabilized chromogen solution. It has a greater sensitivity and produces little or no background staining compared with other alternatives. It is ready to use solution.
Used in immunohistology and immunoblotting as a precipitating substrate for the localization of peroxidase activity. Insoluble end product is resistant to alcohol and fading, making it ideal for immunohistochemistry.
Stabilized Chromogen Solution
This alkaline phosphatase chromogen solution contains the two components in a stabilized solution which may be used as the final step in color development. The resulting product is a permanent, deep-purple stain. It enhances results in both ELISA and immunohistology assays utilizing peroxidase and alkaline phosphatase.
3,3′,5,5′-Tetramethylbenzidine (TMB) is a noncarcinogenic substitute (Ames test negative) for benzidine suitable as peroxidase substrate for use in ELISA procedures. The substrate produces a soluble end product that is pale blue in color and can be read spectrophotometrically at 370 or 620-650 nm. The TMB reaction may be stopped with 2 M H2SO4 (resulting in a yellow color), and read at 450 nm. A sensitive and specific reagent for the detection of blood, assay of hemoglobin, assay of peroxidases.
Prepared from chicken egg white by Ion exchange.
Albumins are a group of acidic proteins which occur plentifully in the body fluids and tissues of mammals and in some plant seeds.
Lyophilized
This albumin is prepared from rat serum.
Transferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains.
Transferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains.
Tested negative for the presence of Hepatitis B Surface Antigen (HBsAg), HIV I/II, HIV-1Ag, HCV, ALT and Syphilis
Tested negative for the presence of Hepatitis B Surface Antigen (HBsAg), HIV I/II, HIV-1Ag, HCV, ALT and Syphilis
ALBUMIN, HUMAN is recommended for use in absorption, distribution, metabolism, and excretion (ADME) pharmacological research; cell culture; drug delivery research; and cryopreservation of cells. Prepared using Cohn method IV. The material is non-reactive for HbsAg, Anti-HCV 3.0, Anti-HIV-1/2 and STS (RPR). This material is also negative for HIV-1 and HCV by PCR. Product Description Albumins are a group of simple proteins found in the body fluids and tissues of animals, and in some plant seeds. It is a single polypeptide chain with one free sulfhydryl group (Cys34) and 17 intrachain disulfide bonds. Biochem/physiol Actions Albumins are soluble monomeric proteins found in the body fluids and tissues of animals and in some plant seeds. Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones. Serum albumins are also vital in regulating the colloidal osmotic pressures of blood.
This human protein is prepared by a modification of the Cohn procedure. Albumin may be used to eliminate background interference in ELISA’s or other enzyme assay systems. It is also used in absorption, distribution, metabolism, and excretion (ADME) pharmacological research; cell culture; drug delivery research; and cryopreservation of cells. Human and bovine albumins contain 16% nitrogen and are often used as standards in protein calibration studies. Due to their free hydrophobic region fatty acid free albumins are used to solubilize lipids in tissue culture, and are also used as blocking agents in Western blots or ELISA applications. Globulin free albumins are suitable for use in applications where no other proteins should be present (e.g., electrophoresis). Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones, and is vital in regulating the colloidal osmotic pressures of blood. Albumin is also seen to bind to exogenous substances, particularly drugs (e.g., ibuprofen, warfarin), and strongly influence their pharmacokinetics. Oxidative stress leading to changes in the redox state of albumin has widely varied effects on its physiological function.