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Bromo-PEG3-azide is a PEG (polyethylene glycol) linker that features a bromide group and an azide group. This molecule is characterized by its hydrophilic PEG spacer, which enhances its solubility in aqueous media. The presence of the azide group allows for reactions with alkyne, BCN, and DBCO through Click Chemistry, resulting in the formation of a stable triazole linkage. Additionally, the bromide (Br) acts as an effective leaving group, facilitating nucleophilic substitution reactions.

1446282-43-4

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1446282-43-4 Usage

Uses

Used in Bioconjugation:
Bromo-PEG3-azide is used as a bioconjugation agent for the attachment of biomolecules to various surfaces or other molecules. The expression is: Bromo-PEG3-azide is used as a bioconjugation agent for the attachment of biomolecules to surfaces or other molecules due to its ability to undergo nucleophilic substitution reactions and form stable triazole linkages through Click Chemistry.
Used in Drug Delivery Systems:
In the pharmaceutical industry, Bromo-PEG3-azide is utilized as a component in drug delivery systems. The expression is: Bromo-PEG3-azide is used as a component in drug delivery systems for its ability to enhance solubility and facilitate targeted drug delivery through bioconjugation and stable linkage formation.
Used in Material Science:
Bromo-PEG3-azide is employed in material science as a modifier to improve the properties of various materials. The expression is: Bromo-PEG3-azide is used as a modifier in material science to enhance material properties, such as solubility and reactivity, through its hydrophilic PEG spacer and reactive functional groups.
Used in Chemical Synthesis:
In the field of chemical synthesis, Bromo-PEG3-azide serves as an intermediate or building block for the creation of more complex molecules. The expression is: Bromo-PEG3-azide is used as an intermediate or building block in chemical synthesis for its versatility in undergoing nucleophilic substitution reactions and forming stable triazole linkages.

Check Digit Verification of cas no

The CAS Registry Mumber 1446282-43-4 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,4,6,2,8 and 2 respectively; the second part has 2 digits, 4 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 1446282-43:
(9*1)+(8*4)+(7*4)+(6*6)+(5*2)+(4*8)+(3*2)+(2*4)+(1*3)=164
164 % 10 = 4
So 1446282-43-4 is a valid CAS Registry Number.

1446282-43-4Downstream Products

1446282-43-4Relevant articles and documents

Recognition of concanavalin a by cationic glucosylated liposomes

Mauceri, Alessandro,Borocci, Stefano,Galantini, Luciano,Giansanti, Luisa,Mancini, Giovanna,Martino, Antonio,Salvati Manni, Livia,Sperduto, Claudio

, p. 11301 - 11306 (2014)

The specificity of carbohydrate-lectin interaction has been reported as an attractive strategy for drug delivery in cancer therapy because of the high levels of lectins in several human malignancies. A novel cationic glucosylated amphiphile was therefore

Protein Modification at Tyrosine with Iminoxyl Radicals

Ishiyama, Takashi,Kanai, Motomu,Maruyama, Katsuya,Oisaki, Kounosuke,Sakai, Kentaro,Seki, Yohei,Togo, Takaya

supporting information, p. 19844 - 19855 (2021/11/30)

Post-translational modifications (PTMs) of proteins are a biological mechanism for reversibly controlling protein function. Synthetic protein modifications (SPMs) at specific canonical amino acids can mimic PTMs. However, reversible SPMs at hydrophobic amino acid residues in proteins are especially limited. Here, we report a tyrosine (Tyr)-selective SPM utilizing persistent iminoxyl radicals, which are readily generated from sterically hindered oximes via single-electron oxidation. The reactivity of iminoxyl radicals with Tyr was dependent on the steric and electronic demands of oximes; isopropyl methyl piperidinium oxime 1f formed stable adducts, whereas the reaction of tert-butyl methyl piperidinium oxime 1o was reversible. The difference in reversibility between 1f and 1o, differentiated only by one methyl group, is due to the stability of iminoxyl radicals, which is partly dictated by the bond dissociation energy of oxime O-H groups. The Tyr-selective modifications with 1f and 1o proceeded under physiologically relevant, mild conditions. Specifically, the stable Tyr-modification with 1f introduced functional small molecules, including an azobenzene photoswitch, to proteins. Moreover, masking critical Tyr residues by SPM with 1o, and subsequent deconjugation triggered by the treatment with a thiol, enabled on-demand control of protein functions. We applied this reversible Tyr modification with 1o to alter an enzymatic activity and the binding affinity of a monoclonal antibody with an antigen upon modification/deconjugation. The on-demand ON/OFF switch of protein functions through Tyr-selective and reversible covalent-bond formation will provide unique opportunities in biological research and therapeutics.

PSMA-TARGETING AMANITIN CONJUGATES

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Paragraph 00171, (2019/04/16)

The invention relates to a PSMA-targeting conjugate comprising (a) an amatoxin; (b) a small molecule PSMA-targeting moiety; and (c) optionally a linker linking said amatoxin and said small molecule PSMA-targeting moiety. The invention furthermore relates to a pharmaceutical composition comprising such conjugate.

Development and evaluation of a non-peptidic ligand for the molecular imaging of inflammatory processes using S100A9 (MRP14) as a novel target

Faust,V?ller,Busch,Sch?fers,Roth,Hermann,Vogl

, p. 15637 - 15640 (2015/11/02)

The establishment of novel molecular imaging tools to monitor the local activity of inflammation remains an interdisciplinary challenge. Our target, the alarmin S100A9, one subunit of the heterodimer S100A8/S100A9 (calprotectin), is locally secreted in hi

BCR-ABL TYROSINE-KINASE LIGANDS CAPABLE OF DIMERIZING IN AN AQUEOUS SOLUTION, AND METHODS OF USING SAME

-

, (2015/07/23)

Described herein are monomers capable of forming a biologically useful multimer when in contact with one, two, three or more other monomers in an aqueous media. In one aspect, such monomers may be capable of binding to another monomer in an aqueous media (e.g. invivo) to form a multimer (e.g. a dimer). Contemplated monomers may include a ligand moiety, a linker element, and a connector element that joins the ligand moiety and the linker element. In an aqueous media, such contemplated monomers may join together via each linker element and may thus be capable of modulating one or more biomolecules substantially simultaneously, e.g., modulate two or more binding sites on a Bcr-Abl tyrosine kinase.

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