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SML3484

Sigma-Aldrich

Biotin-XX-tyramide

≥95% (HPLC)

Synonyme(s) :

1H-Thieno[3,4-d]imidazole-4-pentanamide, hexahydro-N-[6-[[6-[[2-(4-hydroxyphenyl)ethyl]amino]-6-oxohexyl]amino]-6-oxohexyl]-2-oxo-, (3aS,4S,6aR)- (9CI, ACI), Biotin-Ahx-AhxX-phenol, Biotin-Ahx-AhxX-tyramide, Biotin-LC-LC-tyramide, Biotin-XX-Tyr; BxxP, Biotin-XX-phenol

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About This Item

Formule empirique (notation de Hill):
C30H47N5O5S
Numéro CAS:
851113-28-5
Poids moléculaire :
589.79
Numéro MDL:
MFCD34180839
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77

Niveau de qualité

100

Pureté

≥95% (HPLC)

Forme

powder

Conditions de stockage

desiccated

Couleur

white to off-white

Température de stockage

-10 to -25°C

Actions biochimiques/physiologiques

Biotin-XX-tyramide (biotin-XX-phenol; BxxP) is a membrane-impermeant variant of the proximity labeling probe biotin-tyramide (biotin-phenol; BP) that corresponds to BP with a long and polar polyamide linker. Similary to BP, BxxP gives robust biotinylation with HRP and H2O2, but unlike BP, BxxP no longer enters cells, yielding selective labeling of cell surface, but not intracellular, proteins.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Sam Kint et al.
Nucleic acids research, 49(8), e43-e43 (2021-01-30)
Characterization of the epigenetic status of individual cells remains a challenge. Current sequencing approaches have limited coverage, and it is difficult to assign an epigenetic status to the transcription state of individual gene alleles in the same cell. To address
Santosh Renuse et al.
Journal of the American Society for Mass Spectrometry, 31(2), 394-404 (2020-01-16)
The use of biotin or biotin-containing reagents is an essential component of many protein purification and labeling technologies. Owing to its small size and high affinity to the avidin family of proteins, biotin is a versatile molecular handle that permits
Ken H Loh et al.
Cell, 166(5), 1295-1307 (2016-08-28)
Cellular compartments that cannot be biochemically isolated are challenging to characterize. Here we demonstrate the proteomic characterization of the synaptic clefts that exist at both excitatory and inhibitory synapses. Normal brain function relies on the careful balance of these opposing
Jiefu Li et al.
Cell, 180(2), 373-386 (2020-01-21)
Molecular interactions at the cellular interface mediate organized assembly of single cells into tissues and, thus, govern the development and physiology of multicellular organisms. Here, we developed a cell-type-specific, spatiotemporally resolved approach to profile cell-surface proteomes in intact tissues. Quantitative
Sebastian Ols et al.
Cell reports, 30(12), 3964-3971 (2020-03-27)
Although intramuscular (i.m.) administration is the most commonly used route for licensed vaccines, subcutaneous (s.c.) delivery is being explored for several new vaccines under development. Here, we use rhesus macaques, physiologically relevant to humans, to identify the anatomical compartments and

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