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Merck

M8527

Sigma-Aldrich

4-Methylumbelliferyl α-L-Fucopyranosid

fluorogenic, ≥97% (TLC), powder

Synonym(e):

4-Methylumbelliferyl alpha-L-fucopyranoside

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About This Item

Empirische Formel (Hill-System):
C16H18O7
CAS-Nummer:
Molekulargewicht:
322.31
Beilstein:
8160514
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
PubChem Substanz-ID:
NACRES:
NA.21

product name

4-Methylumbelliferyl α-L-Fucopyranosid, ≥97% (TLC)

Assay

≥97% (TLC)

Form

powder

Löslichkeit

DMF: 100 mg/mL, clear, colorless to faintly yellow

Fluoreszenz

λex 360 nm; λem 449 nm (Reaction product)

Lagertemp.

−20°C

SMILES String

C[C@@H]1O[C@@H](Oc2ccc3C(C)=CC(=O)Oc3c2)[C@@H](O)[C@H](O)[C@@H]1O

InChI

1S/C16H18O7/c1-7-5-12(17)23-11-6-9(3-4-10(7)11)22-16-15(20)14(19)13(18)8(2)21-16/h3-6,8,13-16,18-20H,1-2H3/t8-,13+,14+,15-,16-/m0/s1

InChIKey

CQKHENXHLAUMBH-CRLRYRHBSA-N

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Anwendung

4-Methylumbelliferyl α-L-fucopyranoside has been used:
  • as a substrate in α-L-fucosidase 1 (α-L-FUCA-1) enzyme assays to convert it to the fluorescent product 4-methylumbelliferone (4MU) for finding the distribution of the membrane-associated α-L-FUCA-1 of human sperm
  • as a fluorogenic substrate in enzyme assays to evaluate the stability of both the seminal plasma and membrane-associated α-l-fucosidase
  • as a substrate to measure the enzymatic activity of α-L-FUCA-1 of cell extracts from TPC-1, BCPAP, 8505C, and CAL62 cell lines

Substrate

Substrate for α-L-fucosidase

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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M Masserini et al.
The Biochemical journal, 229(3), 595-603 (1985-08-01)
alpha-L-Fucosidase, prepared in highly purified form (Mr 70 000-74 000) from Octopus hepatopancreas, was able to hydrolyse a fucose-containing ganglioside, namely Fuc-GM1 (II3NeuAc,IV2Fuc-GgOse4-Cer). The enzyme showed an irregular kinetic behaviour (v/[S] and v/[E] relationships following sigmoidal curves) when working on
Jennifer J Venditti et al.
Molecular reproduction and development, 74(6), 758-766 (2006-11-30)
Two distinctive isoforms of the enzyme alpha-L-fucosidase are found within human semen in substantial amounts, suggesting specialized functions during reproduction. The membrane-associated isozyme of human sperm cells was previously characterized biochemically, and here we report on its subcellular localization. Intact
A Giuliani et al.
Glycoconjugate journal, 10(6), 447-452 (1993-12-01)
The behaviour of a highly purified alpha-L-fucosidase (E.C. 3.2.1.51) extracted from octopus hepatopancreas was studied with phospholipid vesicles composed of phosphatidylcholine (PC) and phosphatidylserine (PS) containing the fucosylated ganglioside FucGM1, a potential natural substrate of the enzyme. The substrate recognition

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