H9890
HA-Ultrogel®
40% (by weight), aqueous ethanol suspension, 60-180 μm
Synonym(s):
Hydroxyapatite preparation
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About This Item
Recommended Products
form
aqueous ethanol suspension
concentration
40% (by weight)
particle size
60-180 μm
pH
4-13
storage temp.
2-8°C
Application
HA ultrogel is used in affinity chromatography, protein chromatography and adsorption/partition.
Other Notes
Microcrystalline hydroxyapatite in cross-linked 4% beaded agarose
Physical form
Suspension in 1 M NaCl containing 20% ethanol
Legal Information
Ultrogel is a registered trademark of Pall Corporation
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Flam. Liq. 3
Storage Class Code
3 - Flammable liquids
WGK
WGK 3
Flash Point(F)
104.0 °F
Flash Point(C)
40 °C
Certificates of Analysis (COA)
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Purification and characterization of the acid lipase from the endosperm of castor oil seeds.
Journal of Plant Physiology, 149(1-2), 23-29 (1996)
Applied and environmental microbiology, 63(9), 3432-3437 (2006-03-15)
To investigate why Rhizobium sp. (Cicer) strain CC 1192 cells accumulate poly-R-3-hydroxybutyrate in the free-living state but not as bacteroids in nodules on chickpea (Cicer arietinum L.) plants, we have examined the kinetic properties of acetyl coenzyme A (acetyl-CoA) acetyltransferase
The Biochemical journal, 331 ( Pt 2), 649-657 (1998-06-11)
The catalytic domain of p72(syk) kinase (CDp72(syk)) was purified from a 30000 g particulate fraction of rat spleen. The purification procedure employed sequential chromatography on columns of DEAE-Sephacel and Superdex-200, and elution from HA-Ultrogel by chloride. The analysis of the
Plant physiology, 112(4), 1513-1522 (1996-12-01)
Neutral and alkaline invertase were identified in cells of a suspension culture of carrot (Daucus carota L.) and purified to electrophoretic homogeneity. Neutral invertase is an octamer with a molecular mass of 456 kD and subunits of 57 kD, whereas
European journal of biochemistry, 270(15), 3168-3173 (2003-07-19)
Salt-active acharan sulfate lyase (no EC number) has been purified from Bacteroides stercoris HJ-15, which was isolated from human intestinal bacteria with GAG degrading enzymes. The enzyme was purified to apparent homogeneity by a combination of QAE-cellulose, diethylaminoethyl (DEAE)-cellulose, CM-Sephadex
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