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Citas y referencias (57)
Invitrogen™
Estreptavidina agarosa, suspensión granulada sedimentada
La estreptavidina conjugada con agarosa granulada al 4 % entrecruzada se puede utilizar para aislar proteínas biotiniladas. Además, los anticuerposMás información
| Número de catálogo | Cantidad |
|---|---|
| S951 | 5 ml |
Número de catálogo S951
Precio (MXN)
-
Cantidad:
5 ml
La estreptavidina conjugada con agarosa granulada al 4 % entrecruzada se puede utilizar para aislar proteínas biotiniladas. Además, los anticuerpos biotinilados se pueden unir a estreptavidina agarosa para generar matrices de afinidad para el aislamiento de antígenos a gran escala.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Tipo de columnaAfinidad
Etiqueta o tinteAgarosa
Cantidad5 ml
Condiciones de envíoHielo húmedo
Fase estacionariaEstreptavidina
FormularioSuspensión líquida
TipoAgarosa
Unit SizeEach
Contenido y almacenamiento
Almacenar en refrigerador (de 2–8 °C).
Preguntas frecuentes
What is the binding capacity of streptavidin agarose?
Citations & References (57)
Citations & References
Abstract
Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation.
Journal:Anal Biochem
PubMed ID:12419349
'The high-affinity binding of biotin to avidin, streptavidin, and related proteins has been exploited for decades. However, a disadvantage of the biotin/biotin-binding protein interaction is that it is essentially irreversible under physiological conditions. Desthiobiotin is a biotin analogue that binds less tightly to biotin-binding proteins and is easily displaced by
Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH.
Journal:Anal Biochem
PubMed ID:10906242
'A procedure for detecting proteins that contain H(2)O(2)-sensitive cysteine (or selenocysteine) residues was developed as a means with which to study protein oxidation by H(2)O(2) in cells. The procedure is based on the facts that H(2)O(2) and biotin-conjugated iodoacetamide (BIAM) selectively and competitively react with cysteine residues that exhibit a
Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.
Journal:J Cell Biol
PubMed ID:12147673
'Amyloid beta-peptide (Abeta) is generated by the consecutive cleavages of beta- and gamma-secretase. The intramembraneous gamma-secretase cleavage critically depends on the activity of presenilins (PS1 and PS2). Although there is evidence that PSs are aspartyl proteases with gamma-secretase activity, it remains controversial whether their subcellular localization overlaps with the cellular
Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport.
Journal:J Cell Biol
PubMed ID:11425878
'Despite the existence of multiple subunit isoforms for the microtubule motor cytoplasmic dynein, it has not yet been directly shown that dynein complexes with different compositions exhibit different properties. The 14-kD dynein light chain Tctex-1, but not its homologue RP3, binds directly to rhodopsin''s cytoplasmic COOH-terminal tail, which encodes an
Evidence for allosteric linkage between exosites 1 and 2 of thrombin.
Journal:J Biol Chem
PubMed ID:9325262
'Investigations to date have demonstrated that ligand binding to exosites 1 or 2 on thrombin produces conformational changes at the active site. In this study, we directly compared the effect of ligand binding to exosites 1 and 2 on the structure and function of the active site of thrombin and