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A7791 Sigma-Aldrich

N-Acetyl-D-lactosamine

≥98%

Synonym: β-D-Gal-(1→4)-D-GlcNAc, 2-Acetamido-2-deoxy-4-O-β-D-galactopyranosyl-D-glucopyranose, LN, N-Acetyl-4-O-(β-D-galactopyranosyl)-D-glucosamine

  • CAS Number 32181-59-2

  • Empirical Formula (Hill Notation) C14H25NO11

  • Molecular Weight 383.35

  •  Beilstein/REAXYS Number 96808

  •  MDL number MFCD00063785

  •  PubChem Substance ID 24891280

  •  NACRES NA.25

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Properties

Related Categories Biochemicals and Reagents, Carbohydrates, Carbohydrates A to Z, Carbohydrates A-C, Glycan Component Classes,
Quality Level   100
assay   ≥98%
form   powder
optical activity   [α]25/D 27.5 to 32.5 °, c = 0.5% (w/v) in water
application(s)   thin layer chromatography (TLC): suitable
storage temp.   −20°C
SMILES string   CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O)[C@H]2O)[C@@H]1O
InChI   1S/C14H25NO11/c1-4(18)15-7-9(20)12(6(3-17)24-13(7)23)26-14-11(22)10(21)8(19)5(2-16)25-14/h5-14,16-17,19-23H,2-3H2,1H3,(H,15,18)/t5-,6-,7-,8+,9-,10+,11-,12-,13?,14+/m1/s1
InChI key   KFEUJDWYNGMDBV-RPHKZZMBSA-N

Description

Application

N-Acetyl-D-lactosamine is used as a specific lectin target molecule in the identification and differentiation of sugar binding molecules such as the galectins. N-Acetyl-D-lactosamine is used in studies of galactosidase, fucosyltransferase, sialyltransferase, and lectin inhibition.

Useful in studies of galactosidase, fucosyltransferase, sialyltransferase, and lectin inhibition.

Packaging

10 mg in autosample vial

Preparation Note

Synthetic

Safety & Documentation

Safety Information

Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

Articles

O-Glycans

O-Linked Neutral Glycans O-Linked Sialylated Glycans Blood Group Antigens Lewis and Cell Adhesion Glycans α-Gal-(1→3)-Gal Antigens
Glycobiology Analysis Manual, 2nd Edition
Keywords: Adhesion, Catalysis, Coagulation, Degradations, Environmental, Events, Gene expression, Glycosylations, Inflammation, Ligands, O-linked glycosylation, Phosphorylations, Sequences, Transcription, Type

Peer-Reviewed Papers
15

References

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