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1-[(bromoacetyl)oxy]pyrrolidine-2,5-dione is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • 133481-33-1 Structure
  • Basic information

    1. Product Name: 1-[(bromoacetyl)oxy]pyrrolidine-2,5-dione
    2. Synonyms: 1-(2-Bromoacetoxy)-2,5-pyrrolidinedione; 1-(2-Bromoacetoxy)pyrrolidine-2,5-dione; 2,5-Pyrrolidinedione, 1-((bromoacetyl)oxy)-; 2,5-pyrrolidinedione, 1-[(2-bromoacetyl)oxy]-
    3. CAS NO:133481-33-1
    4. Molecular Formula: C6H6BrNO4
    5. Molecular Weight: 236.0201
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 133481-33-1.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: 291.7°C at 760 mmHg
    3. Flash Point: 130.2°C
    4. Appearance: N/A
    5. Density: 1.85g/cm3
    6. Vapor Pressure: 0.00191mmHg at 25°C
    7. Refractive Index: 1.565
    8. Storage Temp.: N/A
    9. Solubility: N/A
    10. CAS DataBase Reference: 1-[(bromoacetyl)oxy]pyrrolidine-2,5-dione(CAS DataBase Reference)
    11. NIST Chemistry Reference: 1-[(bromoacetyl)oxy]pyrrolidine-2,5-dione(133481-33-1)
    12. EPA Substance Registry System: 1-[(bromoacetyl)oxy]pyrrolidine-2,5-dione(133481-33-1)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 133481-33-1(Hazardous Substances Data)

133481-33-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 133481-33-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,3,4,8 and 1 respectively; the second part has 2 digits, 3 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 133481-33:
(8*1)+(7*3)+(6*3)+(5*4)+(4*8)+(3*1)+(2*3)+(1*3)=111
111 % 10 = 1
So 133481-33-1 is a valid CAS Registry Number.

133481-33-1Relevant articles and documents

Conjugates of polyhedral boron compounds with carbohydrates 8. Synthesis and properties of nido-ortho-carborane glycoconjugates containing one to three β-lactosylamine residues

Likhosherstov, L. M.,Novikova, O. S.,Chizhov, A. O.,Sivaev, I. B.,Bregadze, V. I.

, p. 2359 - 2364,6 (2011)

β-Lactosylamine derivatives containing one to three disaccharide residues with the bromine atom at the terminal position of aglycon were synthesized. Conjugation of these derivatives with 1-mercapto-1,2-dicarba-closo- dodecaborane was carried out in DMSO, which was accompanied by deboronation to form nido-ortho-carborane (7,8-dicarba-nido-undecaborate) glycoconjugates in up to 70% yield. The hydrolytic stability of glycoconjugates and the binding efficiency of their triethylammonium salts to castor-bean galectin (Ricinus communis aggluinin, RCA120) were estimated. Glycoconjugates are decomposed in an aqueous solution by ~15% at 37°C in three days. The glycoconjugate salt with one β-lactosylamine residue binds to galectin analogously to lactose; after indroduction of the second β-lactosylamine residue into glycoconjugate, the binding efficiency increases ~6-fold due to the cluster effect.

Conjugation of oligonucleotides via an electrophilic tether: N- chloroacetamidohexyl phosphoramidite reagent

Guzaev, Andrei,Manoharan, Muthiah

, p. 3671 - 3676 (1998)

A novel method for the preparation of oligonucleotides conjugated with nucleophilic ligands is described. A new phosphoramidite building block derived from N-chloroacetyl-6-aminohexanol is attached at the 5'-terminus on the last step of oligonucleotide synthesis. Postsynthesis treatment of support-bound modified oligonucleotide with a variety of amines and mercaptans affords conjugates in high yield.

Kinetic studies and predictions on the hydrolysis and aminolysis of esters of 2-S-phosphorylacetates

Trmcic, Milena,Hodgson, David R. W.

, p. 732 - 741 (2010)

Background: Heterobifunctional cross-linking agents are useful in both protein science and organic synthesis. Aminolysis of reactive esters in aqueous systems is often used in bioconjugation chemistry, but it must compete against hydrolysis processes. Her

Photo-induced multifunctional cross-linking agent, preparation method and application thereof

-

Paragraph 0160-0161, (2021/03/31)

The invention relates to a photo-induced multifunctional cross-linking agent as shown in a general formula (I), wherein the photo-induced multifunctional cross-linking agent is mainly applied to biomacromolecule interaction, such as protein-protein interaction and protein-nucleic acid interaction. According to the invention, the cross-linking agent can be used in biological samples or cells of cell lysis solutions to capture protein-protein interaction or protein-nucleic acid interaction, and can be applied to subsequent protein enrichment and protein cross-linking mass spectrometry; and the photo-induced multifunctional cross-linking agent has important application potential and practical value in interaction research of biomacromolecules.

A Potent Halogen-Bonding Donor Motif for Anion Recognition and Anion Template Mechanical Bond Synthesis

Bunchuay, Thanthapatra,Docker, Andrew,Martinez-Martinez, Antonio J.,Beer, Paul D.

supporting information, p. 13823 - 13827 (2019/08/22)

The covalent attachment of electron deficient perfluoroaryl substituents to a bis-iodotriazole pyridinium group produces a remarkably potent halogen bonding donor motif for anion recognition in aqueous media. Such a motif also establishes halogen bonding anion templation as a highly efficient method for constructing a mechanically interlocked molecule in unprecedented near quantitative yield. The resulting bis-perfluoroaryl substituted iodotriazole pyridinium axle containing halogen bonding [2]rotaxane host exhibits exceptionally strong halide binding affinities in competitive 50 % water containing aqueous media, by a factor of at least three orders of magnitude greater in comparison to a hydrogen bonding rotaxane host analogue. These observations further champion and advance halogen bonding as a powerful tool for recognizing anions in aqueous media.

Corroboration of Zn(ii)-Mg(ii)-tertiary structure interplays essential for the optimal catalysis of a phosphorothiolate thiolesterase ribozyme

Wang, Tzu-Pin,Su, Yu-Chih,Chen, Yi,Severance, Scott,Hwang, Chi-Ching,Liou, Yi-Ming,Lu, Chia-Hui,Lin, Kun-Liang,Zhu, Rui Jing,Wang, Eng-Chi

, p. 32775 - 32793 (2018/10/15)

The TW17 ribozyme, a catalytic RNA selected from a pool of artificial RNA, is specific for the Zn2+-dependent hydrolysis of a phosphorothiolate thiolester bond. Here, we describe the organic synthesis of both guanosine α-thio-monophosphate and the substrates required for selecting and characterizing the TW17 ribozyme, and for deciphering the catalytic mechanism of the ribozyme. By successively substituting the substrate originally conjugated to the RNA pool with structurally modified substrates, we demonstrated that the TW17 ribozyme specifically catalyzes phosphorothiolate thiolester hydrolysis. Metal titration studies of TW17 ribozyme catalysis in the presence of Zn2+ alone, Zn2+ and Mg2+, and Zn2+ and [Co(NH3)6]3+ supported our findings that Zn2+ is absolutely required for ribozyme catalysis, and indicated that optimal ribozyme catalysis involves the presence of outer-sphere and one inner-sphere Mg2+. A survey of the TW17 ribozyme activity at various pHs revealed that the activity of the ribozyme critically depends on the alkaline conditions. Moreover, a GNRA tetraloop-containing ribozyme constructed with active catalysis in trans provided catalysis and multiple substrate turnover efficiencies significantly higher than ribozymes lacking a GNRA tetraloop. This research supports the essential roles of Zn2+, Mg2+, and a GNRA tetraloop in modulating the TW17 ribozyme structure for optimal ribozyme catalysis, leading also to the formulation of a proposed reaction mechanism for TW17 ribozyme catalysis.

A carbon -13 isotope-labeled bromination phosphine compound and its preparation method and application

-

Paragraph 0043; 0044, (2017/10/31)

The invention relates to a carbon-13 isotope-labeled phosphonium bromide compound as shown in a structural formula (I) as well as a preparation method and application thereof. The carbon-13 isotope-labeled phosphonium bromide compound (C13-TMPP-Ac-OSu) disclosed by the invention is matched with C12-TMPP-Ac-OSu for use, and can be used for identifying the polypeptide through mass spectrometric analysis on de novo sequencing and carrying out quantitative analysis by utilizing the peak intensity of two signals generated in a mass spectrum by a same polypeptide which contains two different labels, thereby realizing the synchronous progress of the de novo sequencing and protein quantitative analysis of the polypeptide; the carbon-13 isotope-labeled phosphonium bromide compound (C13-TMPP-Ac-OSu) disclosed by the invention has the advantages of simple analysis method, good stability and high accuracy.

SITE SELECTIVE CONJUGATION OF AN OLIGONUCLEOTIDE CONJUGATE OR A SMALL MOLECULE TO A METAL BINDING PROTEIN

-

Page/Page column 72, (2016/01/25)

The present invention relates to methods for site selective conjugation of an oligonucleotide conjugate to a metal binding protein comprising a metal binding site and for site selective conjugation of a small molecule conjugation compound (SMCoC) to an antibody comprising a metal binding site, metal binding protein conjugates obtainable by said methods, and uses of said metal binding protein conjugates.

Analyte detection utilizing polynucleotide sequences, composition, process and kit

-

, (2016/01/20)

A method of detecting in a sample an analyte (A) having a molecularly recognizable portion thereon, which comprises: providing (B) a molecular bridging entity having thereon: (i) a portion capable of recognizing the molecularly recognizable portion on the analyte; and (ii) a portion comprising a polynucleotide sequence; and (C) a signalling entity having thereon: (i) a polynucleotide portion capable of annealing to the polynucleotide portion of the bridging entity, thereby to form a stable polynucleotide hybrid, and (ii) a signal generating portion; forming a complex comprising: (1) the analyte (A) complexed through its molecularly recognizable portion to (2) the recognizing portion of the entity (B); the entity (B) being complexed through the polynucleotide portion thereon to (3) the polynucleotide portion of the signalling entity; and detecting a signal by means of the signal generating portion present in the complex.

PEGylation of the peptide Bac7(1-35) reduces renal clearance while retaining antibacterial activity and bacterial cell penetration capacity

Benincasa, Monica,Zahariev, Sotir,Pelillo, Chiara,Milan, Annalisa,Gennaro, Renato,Scocchi, Marco

supporting information, p. 210 - 219 (2015/03/31)

The proline-rich antibacterial peptide Bac7(1-35) protects mice against Salmonella typhimurium infection, despite its rapid clearance. To overcome this problem the peptide was linked to a polyethylene glycol (PEG) molecule either via a cleavable ester bond or via a non-hydrolysable amide bond. Both the PEGylated conjugates retained most of the in vitro activity against S. typhimurium. In addition, the ester bond was cleaved in human serum or plasma, releasing a carboxymethyl derivative of Bac7(1-35) which accounts for a higher activity of this peptide with relative to the other, non-hydrolysable form. Both PEGylated peptides maintained the capacity of the unconjugated form to kill bacteria without permeabilizing the bacterial membranes, by penetrating into cells. They exploited the same transporter as unmodified Bac7(1-35), suggesting it has the capacity to internalize quite sizeable cargo if this is linked to Bac7 fragment. PEGylation allows the peptide to have a wide distribution in mice, and a slow renal clearance, indicating that this strategy would improve the bioavailability of Bac7, and in principle of other antimicrobial peptides. This can be an equally important issue to reducing cytotoxicity for therapeutic use of these antibacterials.

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