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Merck

SML3484

Biotin-XX-tyramide

≥95% (HPLC), membrane-impermeant biotin label, powder

Sinônimo(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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Sobre este item

Fórmula empírica (Notação de Hill):
C30H47N5O5S
Número CAS:
Peso molecular:
589.79
UNSPSC Code:
12352200
NACRES:
NA.77
MDL number:

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Nome do produto

Biotin-XX-tyramide, ≥95% (HPLC)

assay

≥95% (HPLC)

form

powder

storage condition

desiccated

color

white to off-white

storage temp.

-10 to -25°C

Quality Level

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Este Item
SML2135H1759913863
assay

≥95% (HPLC)

assay

≥97% (HPLC)

assay

≥98% (HPLC)

assay

-

form

powder

form

powder

form

powder

form

powder

Quality Level

100

Quality Level

-

Quality Level

200

Quality Level

100

storage temp.

-10 to -25°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage condition

desiccated

storage condition

-

storage condition

-

storage condition

-

color

white to off-white

color

white to beige

color

white to off-white

color

-

Biochem/physiol Actions

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.
Membrane-impermeant variant of biotin-phenol biotin-tyramide (biotin-phenol; BP) for proximity labeling of cell surface, but not intracellular, proteins.

Classe de armazenamento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_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
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
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
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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