≥95%, Potency:≤10IU/mg for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
Store at -20°C,Argon charged Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Heparan Sulfate (HS) is a class of sulfated GAGs composed of disaccharide units (GlcUA/IdoUA β/α 1-4GlcNAc) composed of glucuronic acid (GlcUA)/iduronic acid (IdoUA) and N-acetylglucosamine (GlcNAc), which are repeatedly linked by α -1,4-glycosidic bonds. In biosynthesis, HS covalently binds to core proteins to form proteoglycans (HSPGs), which are widely expressed on the cell surface and extracellular matrix; GlcUA can undergo differential isomerization to form IdoUA, and under the action of various sulfate transferases, the N, C6, and C3 positions of GlcNAc and the C2 position of GlcUA in the HS chain are sulfated to form highly complex HS side chains. Compared with heparin (Hep), HS has a more complex structure, manifested by more diverse sulfurization modes, lower IdoA content, and longer polysaccharide chains. The HS polysaccharide chain can be roughly divided into three parts: the NA region, which is the region without sulfation modification; In the NS region, the GlcNAc residues in the disaccharide units have undergone deacetylation and sulfation modifications; The NA/NS region is a mixed region of NA and NS, where many sulfation and isomerization modifications in HS occur. HS participates in various physiological and pathological processes such as growth, development, and disease occurrence through interactions with growth factors, cytokines, matrix proteins, etc.
Comprehensive hazard, handling, storage, and regulatory compliance document.
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View spec sheet →| Sensitivity | Moisture sensitive |
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I2511786