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Key Documents

437641

Sigma-Aldrich

Lipoproteins, High Density, Human Plasma

Synonym(s):

HDL

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.25

assay

≥95% (of total lipoprotein content, electrophoresis)

Quality Level

form

liquid

manufacturer/tradename

Calbiochem®

storage condition

do not freeze

shipped in

wet ice

storage temp.

2-8°C

General description

A 10 mg vial contains ~5 mg of protein.
Native high density lipoproteins from human plasma. Cholesterol-carrier lipoprotein that acts as scavenger of tissue cholesterol. Important in cholesterol efflux from tissues. Involved in return of cholesterol from the periphery to the liver for removal as bile acids. Composition: 55-45% lipid, 45-55% protein.
Native high density lipoproteins from human plasma. Cholesterol-carrier protein that acts as a scavenger of tissue cholesterol. Important in cholesterol efflux from tissues. Involved in return of cholesterol from the periphery to the liver for removal as bile acids. (Composition: 55-45% lipid, 45-55% protein. Note: 10 mg vial contains 5 mg of protein.)

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Other Notes

Badimon, J.J., et al. 1992. Circulation 86, III86.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Xu Cui et al.
Stroke, 41(9), 2044-2049 (2010-07-31)
Niacin is the most effective medication in current clinical use for increasing high-density lipoprotein cholesterol. We tested the hypothesis that niacin treatment of stroke promotes synaptic plasticity and axon growth in the ischemic brain. Male Wistar rats were subjected to
Wojciech Paslawski et al.
Proceedings of the National Academy of Sciences of the United States of America, 116(30), 15226-15235 (2019-07-05)
The progressive accumulation, aggregation, and spread of α-synuclein (αSN) are common hallmarks of Parkinson's disease (PD) pathology. Moreover, numerous proteins interact with αSN species, influencing its toxicity in the brain. In the present study, we extended analyses of αSN-interacting proteins

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