71610-M
D-Desthiobiotin
Sinónimos:
5-methyl-2-oxo-4-imidazolidinehexanoic acid, 5-methyl-2-oxo-4-imidazoline-caproic acid, 6-(5-methyl-2-oxo-imidazolidin-4-yl)hexanoic acid, Dethiobiotin
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About This Item
UNSPSC Code:
41106500
NACRES:
NA.56
Productos recomendados
form
solid
manufacturer/tradename
Novagen®
storage condition
OK to freeze
storage temp.
2-8°C
Categorías relacionadas
General description
D-Desthiobiotin provides a gentle elution of Strep•Tag II proteins from the biotin-binding site of Strep•Tactin resins. The D-Desthiobiotin is offered as a lyophilized powder for preparation of elution buffer.
Application
D-Desthiobiotin has been used to elute recombinant strap-tag proteins bound to Strep-Tactin superflow high capacity resin.
Biochem/physiol Actions
D-Desthiobiotin is an analog of biotin. It is a non-sulfur metabolite and a biotin precursor. It displays lower binding towards biotin-binding proteins when compared to biotin.
Components
•: 1 g: D-Desthiobiotin
Warning
Toxicity: Standard Handling (A)
Legal Information
NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Philip A Band et al.
Protein expression and purification, 71(1), 62-73 (2010-01-05)
Work from multiple laboratories has clarified how the structural domains of botulinum neurotoxin A (BoNT/A) disable neuronal exocytosis, but important questions remain unanswered. Because BoNT/A intoxication disables its own uptake, light chain (LC) does not accumulate in neurons at detectable
Jessica Marcandalli et al.
Cell, 176(6), 1420-1431 (2019-03-09)
Respiratory syncytial virus (RSV) is a worldwide public health concern for which no vaccine is available. Elucidation of the prefusion structure of the RSV F glycoprotein and its identification as the main target of neutralizing antibodies have provided new opportunities
James D Hirsch et al.
Analytical biochemistry, 308(2), 343-357 (2002-11-07)
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
Nadia Martinez-Martin et al.
Cell, 174(5), 1158-1171 (2018-07-31)
Characterizing cell surface receptors mediating viral infection is critical for understanding viral tropism and developing antiviral therapies. Nevertheless, due to challenges associated with detecting protein interactions on the cell surface, the host receptors of many human pathogens remain unknown. Here
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