Biotina azida (PEG4 carboxamida-6-azidohexanilo biotina)
Biotina azida (PEG4 carboxamida-6-azidohexanilo biotina)
Invitrogen™

Biotina azida (PEG4 carboxamida-6-azidohexanilo biotina)

El hapteno y la biotina azida son reactivos con los alquinos de terminales mediante una reacción de clic catalizada porMás información
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Número de catálogoCantidad
B101841 mg
Número de catálogo B10184
Precio (MXN)
-
Cantidad:
1 mg
El hapteno y la biotina azida son reactivos con los alquinos de terminales mediante una reacción de clic catalizada por cobre. La biotina se puede detectar posteriormente con estreptavidina, avidina o la proteína de unión de biotina NeutrAvidin®.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaAlquino
FormatoSólido
Etiqueta o tinteBiotina
Peso molecular615,79 Da
Tipo de productoAzida de biotina
Cantidad1 mg
Grupo reactivoAzida
Fracción reactivaAmina, azida
Condiciones de envíoTemperatura ambiente
SolubilidadDMSO (dimetilsulfóxido)
ColorBiotina
Tipo de etiquetaBiotina y otros haptenos
Línea de productosMolecular Probes
Unit SizeEach
Contenido y almacenamiento
Almacénelo a ≤-20 °C y manténgalo desecado.

Citations & References (12)

Citations & References
Abstract
AID-induced decrease in topoisomerase 1 induces DNA structural alteration and DNA cleavage for class switch recombination.
Authors:Kobayashi M, Aida M, Nagaoka H, Begum NA, Kitawaki Y, Nakata M, Stanlie A, Doi T, Kato L, Okazaki IM, Shinkura R, Muramatsu M, Kinoshita K, Honjo T,
Journal:Proc Natl Acad Sci U S A
PubMed ID:20018730
'To initiate class switch recombination (CSR) activation-induced cytidine deaminase (AID) induces staggered nick cleavage in the S region, which lies 5'' to each Ig constant region gene and is rich in palindromic sequences. Topoisomerase 1 (Top1) controls the supercoiling of DNA by nicking, rotating, and religating one strand of DNA. ... More
Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives.
Authors:Vila A, Tallman KA, Jacobs AT, Liebler DC, Porter NA, Marnett LJ,
Journal:Chem Res Toxicol
PubMed ID:18232660
'Polyunsaturated fatty acids (PUFA) are primary targets of free radical damage during oxidative stress. Diffusible electrophilic alpha,beta-unsaturated aldehydes, such as 4-hydroxynonenal (HNE), have been shown to modify proteins that mediate cell signaling (e.g., IKK and Keap1) and alter gene expression pathways responsible for inducing antioxidant genes, heat shock proteins, and ... More
A concomitant loss of dormant origins and FANCC exacerbates genome instability by impairing DNA replication fork progression.
Authors:Luebben SW, Kawabata T, Johnson CS, O'Sullivan MG, Shima N,
Journal:
PubMed ID:24589582
'Accumulating evidence suggests that dormant DNA replication origins play an important role in the recovery of stalled forks. However, their functional interactions with other fork recovery mechanisms have not been tested. We previously reported intrinsic activation of the Fanconi anemia (FA) pathway in a tumor-prone mouse model (Mcm4(chaos3)) with a ... More
Metabolic labeling of sialic acids in living animals with alkynyl sugars.
Authors:Chang PV, Chen X, Smyrniotis C, Xenakis A, Hu T, Bertozzi CR, Wu P,
Journal:Angew Chem Int Ed Engl
PubMed ID:19388017
Sialome sweet sialome: As sialic acids are involved in many host-pathogen recognition events and are markers of embryonic and malignant tissues, there is great interest in methods for the enrichment and identification of sialylated glycoproteins from complex tissues. Now N-(4-pentynoyl)mannosamine can be used to metabolically label sialylated glycoproteins in living ... More
Regulation of the Skeletal Muscle Ryanodine Receptor/Ca2+-release Channel RyR1 by S-Palmitoylation.
Authors:Chaube R, Hess DT, Wang YJ, Plummer B, Sun QA, Laurita K, Stamler JS,
Journal:
PubMed ID:24509862
The ryanodine receptor/Ca(2+)-release channels (RyRs) of skeletal and cardiac muscle are essential for Ca(2+) release from the sarcoplasmic reticulum that mediates excitation-contraction coupling. It has been shown that RyR activity is regulated by dynamic post-translational modifications of Cys residues, in particular S-nitrosylation and S-oxidation. Here we show that the predominant ... More