Perflutren

Base Information

• Chemical Name: Perflutren
• CAS No.: 9048-46-8
• Deprecated CAS: 218599-63-4,300408-51-9,300408-51-9
• Molecular Formula: Unspecified
• Molecular Weight: 0
• Hs Code.: 35029000
• European Community (EC) Number: 200-941-9,274-272-6,232-936-2
• UN Number: 2424
• UNII: CK0N3WH0SR
• DSSTox Substance ID: DTXSID9052503
• Nikkaji Number: J353K
• Wikipedia: Octafluoropropane
• Wikidata: Q412659
• NCI Thesaurus Code: C47664,C65218,C74071
• RXCUI: 283753
• Metabolomics Workbench ID: 54478
• ChEMBL ID: CHEMBL1663
• Mol file: 9048-46-8.mol

Synonyms:C3F8-gas;Definity;MRX-115;octafluoropropane;perfluoropropane;perflutren

Chemical Property of Perflutren

Chemical Property:

• Appearance/Colour: COA
• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: 2-8°C
• Solubility.: PBS: >40 mg/mL
• Water Solubility.: Soluble in water.
• XLogP3: 3.1
• Hydrogen Bond Donor Count: 0
• Hydrogen Bond Acceptor Count: 8
• Rotatable Bond Count: 0
• Exact Mass: 187.98722530
• Heavy Atom Count: 11
• Complexity: 120
• Transport DOT Label: Non-Flammable Gas

Purity/Quality:

99.0% ^*data from raw suppliers

Bovine Serum Albumin lyophilized powder, Vitamin B12 deficient ^*data from reagent suppliers

Safty Information:

• Pictogram(s): Xn
• Hazard Codes: Xn
• Statements: 22-52/53-21/22
• Safety Statements: 24/25-61-36/37

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Chemical Classes: UVCB,Other Classes -> Halogenated Aliphatics,Saturated
• Canonical SMILES: C(C(F)(F)F)(C(F)(F)F)(F)F
• Recent ClinicalTrials: An Ascending Dose Comparison of MVT-100 to Definity in Healthy Volunteers
• Recent EU Clinical Trials: Human albumin treatment in adult septic shock. A phase 2, multicenter, randomized, controlled study evaluating the immune response and organ failure.
• Description: Bovine serum albumin is a protein which has a key role in regulating blood colloidal osmotic pressure. A water-soluble protein composed of 583 amino acids, BSA has a calculated molecular weight of 66,430 Daltons. Six α-helices form three homologous domains of BSA. Depending on pH, BSA undergoes reversible conformational isomerization. The native structure of the protein becomes reactive and flexible on heating.This BSA product is specifically evaluated and tested for the following properties:Very low protease content / protease-freeVery low fatty acid content / fatty acid-freeProtease-free BSA is especially useful for applications like:Enzyme assaysProtein-based assaysProtease-sensitive techniques that include:a. Enzyme immunoassay (EIA)b. Nucleic acid hybridizationc. Radioimmunoassay (RIA) Acetylated BSA may be used as a positive control for ELISA or WB when employing an acetyl-lysine monoclonal or polyclonal antibody. Cayman’s Acetyl Lysine Monoclonal Antibody (Clone 7F8) can detect less than 1 ng of this positive control by immunoblotting. Dilutions from a 1 mg/ml stock solution and 2X Laemmli Buffer may be prepared for WB use. For example, dissolve the 1 mg lyophilized protein in 1 ml of purified water (aliquot and freeze for later, use as needed), then make ten-fold dilutions until the desired concentration range is obtained. Finally dilute the product 1:1 in 2X Laemmli Buffer. Incubate the prepared sample for five minutes in boiling water followed by five minutes on ice prior to loading gels.Histone subunit modifications such as lysine acetylation are regulated by the activity of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Epigenetic modifications such as protein acetylation directly influence cellular genetic programs including those contributing to cancer cell viability.
• Uses: Suitable for cell culture media supplement.Bovine serum albumin (BSA) Fraction V has uses in many applications such as stabilizing proteins in solution, blocking non-specific binding in immuno-assays, and as a protein standard in various protein assays.Stabilizer for proteins and enzymes in solutionBlocking agent for immuno-assays (ie, western blot, IHC, IF)Minimizes non-specific antibody bindingIgG- and protease-free50 g of solid powderBovine serum albumin (BSA) is commonly used as a stabilizing agent for proteins and enzymes, including dilute solutions of antibody. It is also used as a blocking agent to reduce non-specific antibody binding in immuno-detection procedures such as western blotting, immunofluorescence, and IHC. It is also suitable for use in protease sensitive assays such as RIA and EIA, as well as nucleic acid hybridization. This BSA is IgG- and protease-free. Select the right albumin for your application with the Albumin Selection GuideBSA has various uses in molecular biology applications, such as:As an added component in solutions of enzymes or of other proteins, to prevent adhesion of the enzyme or other protein of interest to the reaction tube surface or to pipette surfacesAs an inert enzyme or protein stabilizer during incubation, to allow the enzyme or protein of interest to function properly Protease-sensitive Immunoassays such as RIA, EIA, Fluorescent and Chemiluminescent, Protein Standard, Diluent, Protein, Conjugate or Enzyme Stabilizer. Bovine Serum Albumin is applicable for numerous biochemical applications including ELISAs (Enzyme-Linked Immunosorbent Assay), immunoblots, and immunohistochemistry. Frequently used as a blocking reagent; particularly useful with casein-sensitive antibodies, such as phospho-specific antibodies. Also used as a nutrient in cell and microbial culture. In restriction digests, BSA is used to stabilize some enzymes during digestion of DNA and to prevent adhesion of the enzyme to reaction tubes and other vessels. Commonly used to determine the quantity of other proteins, by comparing an unknown quantity of protein to known amounts of BSA. Hybridization, Selected Cell Culture applications

Refernces

Analysis of phosphorylated peptides by double pseudoneutral loss extraction coupled with derivatization using N-(4-bromobenzoyl)aminoethanethiol

10.1021/ac9017988

The research presents a novel strategy for identifying phosphorylated serine and threonine residues in phosphoproteins. The study introduces a new derivatization reagent, N-(4-bromobenzoyl)aminoethanethiol, which selectively reacts with R,γ-unsaturated ketones produced by β-elimination of phosphoryl groups from phosphorylated serine or threonine residues. This reagent contains a bromine atom, which imparts a characteristic isotopic pattern to the mass spectrum of the derivatized peptide, facilitating the identification of phosphorylated peptides. The method involves selective derivatization of phosphoproteins followed by double pseudoneutral loss extraction after nanoLC/ESI-MS/MS analysis. This approach allows for the effective detection of phosphorylated peptides even in complex mixtures, as demonstrated through the analysis of a mixture of various proteins including β-casein and bovine serum albumin. The study highlights the utility of this method in overcoming challenges associated with the low concentration and detection of phosphorylated peptides in complex biological samples.

Molecular engineering of near-infrared light-responsive BODIPY-based nanoparticles with enhanced photothermal and photoacoustic efficiencies for cancer theranostics

10.7150/thno.34418

This study explores the development of small organic molecule-based nanoparticles for cancer treatment and imaging. The researchers designed a heptacyclic B, O-chelated BODIPY structure (Boca-BODIPY) with strong near-infrared (NIR) absorption through molecular engineering. Heavy atoms and alkyl chains were introduced to enhance its photothermal conversion efficiency and interaction with proteins. The Boca-BODIPY molecules were encapsulated in reduced bovine serum albumin (BSA) through self-assembly to improve their aqueous solubility and biocompatibility. The resulting BSA-Boca-BODIPY nanoparticles exhibited excellent biocompatibility, stability, and a high photothermal conversion efficiency of up to 58.7%. They significantly enhanced photoacoustic contrast in tumor regions and efficiently converted laser energy into hyperthermia for tumor ablation under photoacoustic imaging-guided photothermal therapy (PTT). The study demonstrates that molecular engineering is a promising approach to designing organic-molecule-based nanoparticles for cancer theranostics, with potential for future personalized medicine applications.