| Description | Product descriptionCompositionStorage Conditions50T100TSolution ARoom temperature100mL200mLDetox BRoom temperature25g50gAfter the product is received, store the ingredients at the temperature indicated above, and it will be valid for 12 months. Ethidium bromide (EB) Ames test results show that EB Product descriptionCompositionStorage Conditions50T100TSolution ARoom temperature100mL200mLDetox BRoom temperature25g50gAfter the product is received, store the ingredients at the temperature indicated above, and it will be valid for 12 months. Ethidium bromide (EB) Ames test results show that EB can easily cause mutations in organisms. Powerful EB Detoxifier is a product specially designed to remove ethidium bromide (EB) pollution. It can effectively destroy the structure of EB and remove the carcinogenicity of EB, thereby achieving the purpose of cleaning EB pollution. It is suitable for removing EB contamination of electrophoresis buffer, biochemical solution and solid surface (such as laboratory bench, centrifuge, glassware, stainless steel products, etc.). After using a powerful EB detoxifier to treat EB pollutants, then discarding it can protect the environment from EB pollutants.Product performance indexIt can destroy the structure of EB, eliminate the fluorescence of EB, and reduce its mutagenicity by more than 99.5%.Precautions1. Solution A is corrosive, and to protect your safety during the operation of EB, please wear gloves and goggles.2. There may be a small amount of irritating and harmful gas generated during the chemical reagent preparation and processing of EB, please operate in a fume hood.3. There is no method that can eliminate EB 100%, so even after handling, you should wear gloves and handle it carefully, not as 100% safe. If conditions permit, it is best to regularly test for mutagenicity to ensure the correctness of the treatment process.Operation steps: (Please read the notes before experiment)1. Treatment of various pollution solutions (100mL EB pollution solution)1) Ensure that the concentration of EB in various polluted solutions does not exceed 0.5mg/mL. If the concentration is too high, first dilute with water to meet the required concentration.2) Preparation of working solution: In a fume hood, dilute 2 mL of solution A with deionized water to a final volume of 20 mL for use. Dissolve 0.42 g of detoxifier B in water and dilute to 12 mL for use.3) Add the above 20mL solution A working solution and 12mL detoxifier B working solution to 100mL EB contaminated solution, stir and mix carefully (make sure pH≤3).4) Allow to react at room temperature for 24 hours, adjust the pH to 5-9 with sodium bicarbonate.5) Wash the reactants into the water tank with a lot of water for disposal.2. Various solid surface pollution treatment1) Preparation of working solution: In a fume hood, add 4.2g of detoxifier B to 300mL of deionized water, add 20mL of solution A after fully dissolving, stir and mix carefully (pH is about 1.8).2) After ensuring that the electrical appliances are in a power-off state, soak the freshly prepared working fluid with a paper towel, carefully wipe clean the contaminated surface, repeat 6 times, each time change to a new paper towel soaked in the working fluid, and finally soak it clean Wipe clean the working fluid with paper towels of deionized water, and collect the paper towels into a designated processing container. The pH value of the working fluid is 1.8, which is slightly corrosive. It is not suitable for wiping items with weak tolerance. You can use paper towels soaked in deionized water to wipe. Before wiping, a UV lamp can be used to help find the contaminated area. After wiping, it can help confirm that it has been wiped clean.3) Soak these contaminated paper towels in the working fluid at room temperature for at least one hour. After adjusting the pH to 5-9 with sodium bicarbonate, the liquid is flushed into the sink with plenty of water, and the paper towels are put into the garbage dump... Read More | Inquire | Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40) peptides. It has a β-sheet and β-turn structure. 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Alternatively-spliced forms are known to occur, but the most common form is a type I transmembrane protein with a 674 aa extracellular domain (ECD) that includes seven C2-type immunoglobulin domains, a 22 aa transmembrane segment, and a 19 amino acid (aa) cytoplasmic tail. Within the ECD, human VCAM-1 shares 75% and 76% aa sequence identity with the mouse and rat VCAM-1, respectively. VCAM-1 binds to leukocyte integrins alpha 4 beta 1 (VLA-4) and alpha 4 beta 7. During the inflammatory adhesion mechanism, activated integrins halt rolling leukocytes and attach them firmly to the vascular endothelium. The VCAM-1:VLA-4/ alpha 4 beta 7 interaction is also thought to be involved in the extravasation of white blood cells through the blood vessel wall to sites of inflammation. ELISA techniques have shown that detectable levels of soluble VCAM-1 are present in the biological fluids of apparently normal individuals, but elevated levels of serum VCAM-1 are indicative of future Atrial Fibrillation incident as well as liver disease. Tumor cells use overexpression of VCAM-1 as means of escaping immune surveillance.Post-translational modifications：Sialoglycoprotein.Function:Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation... Read More |