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Merck

H6508

Sigma-Aldrich

Heparin−Agarose

Type I, saline suspension

Sinónimos:

Heparin beads, Heparin resin

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About This Item

MDL number:
UNSPSC Code:
23151817
NACRES:
NA.56

biological source

heparin from Porcine intestinal mucosa

Quality Level

type

Type I

form

saline suspension

extent of labeling

400-1500 μg per mL packed gel (activity approx. 140 USP units per mg)

technique(s)

affinity chromatography: suitable

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

1 atom

suitability

suitable for chromatography

storage temp.

2-8°C

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Application

Heparin-agarose is developed from porcine intestinal mucosa and is used in affinity chromatography. Heparin-agarose has been used in studies to provide information on human monocytic ehrlichiosis, tumor necrosis and the effects of coagulation from Vipera snake venom.

Physical form

Suspension in 0.5 M NaCl containing preservative

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Analysis of Adeno-Associated Virus and HPV Interaction.
Hermonat, P.L., et al.
Methods in Molecular Medicine, 119, 397-409 (2006)
91. Universal purification of AAV serotypes 1?5 modified to contain a heparin binding epitope.
Faust, S.M., et al.
Molecular Therapy, 9, S36-S36 (2004)
D A Willins et al.
The Journal of biological chemistry, 266(17), 10768-10774 (1991-06-15)
Exogenous leucine affects the expression of a number of different operons in Escherichia coli. For at least some of these operons, the leucine-related effect is mediated by a protein called Lrp (Leucine-responsive regulatory protein). The purification of Lrp to near
I V Kaplan et al.
Atherosclerosis, 158(2), 455-463 (2001-10-05)
Oxidation of beta-lipoproteins has been linked to the development of arteriosclerosis. Using a copper mediated cell free system to oxidize beta-lipoproteins, we found that beta -lipoproteins isolated from plasma were less susceptible to oxidation than lipoproteins from serum and that
M E Silvestri et al.
Scandinavian journal of immunology, 53(3), 282-289 (2001-03-17)
An investigation was performed into the heparin-binding properties of a synthetic peptide deduced from the sequence of human cytomegalovirus glycoprotein B. The peptide, T7-13:3, amino acids 69-78, which was previously shown to contain a neutralization epitope was able to bind

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