NewsRelease

Cleanascite™Cited In Study of Biomarkers in Psoriasis and Cardiovascular Disease.

MONMOUTHJUNCTION, NJ, December16, 2024 -- Biotech Support Group reports on an article, describingthe simplicity and efficiency of their lipid clearance samplepreparation in a study of HDL-associated Vitamin D Binding Protein(DBP) correlates with disease severity in psoriasis andcardiovascular disease. Thecitation is:

PlayfordM, Li H, Dey A, Florida E, Teague H, Gordon S, Mehta N, HDLassociated Vitamin D Binding Protein levels are Inversely Associatedwith Necrotic Plaque Burden in Psoriasis, Atherosclerosis Plus,https://doi.org/10.1016/j.athplu.2024.12.002.

VitaminD binding protein (DBP) serves a dual function as a vitamin D carrierand actin scavenger. Free DBP (S-DBP) (also known as Gene GC) is anabundant protein in human serum, while a smaller pool is bound tolipoproteins like HDL and VLDL. The role of DBP’s interaction withlipoproteins remains unclear. The investigators sought to comparewhether HDL-associated DBP and/or total serum DBP could serve asuseful biomarkers for assessing disease severity in psoriasis andcardiovascular disease.

Thearticle states “…determine whether DBP was found in HDL particlesor just as a co fractioning protein from chromatography. Fractions 20to 28 were treated with a lipid-removal agent (Cleanascite™), andwhile this treatment removed many of the proteins in fractions 21 to27, the non-lipidated ‘albumin’ fraction remained (fig.1d). Furthermore, phospholipid analysis of fractions 18 to 29 revealedthat 21, 22 and 25, 26 are rich in phospholipid and were removed withCleanascite™ treatment (fig.1f). DBP was readily detected infractions 24 to 27, but mostly removed upon lipid-removal. In thesame conditions, DBP was abundantly detected in fraction 28suggesting that in this fraction, DBP is not bound to lipidatedproteins (fig.1g). At all tested concentrations of DBP, most remainedunbound to the lipid removal agent demonstrating that DBP does notbind to Cleanascite™ in the absence of lipid.” 

Insummary, the data suggests that HDL-DBP may be both protective forinflammatory diseases and vulnerable coronary plaque. Due to DBP’spotential to bind lipids, actin and vitamin D, each of which have arole in CVD, makes it a compelling biomarker warranting furtherinvestigation.

“Thisarticle demonstrates the most important characteristic ofCleanascite™, that it binds only the lipid-bound protein. Whilethere are other lipid removal reagents, they suffer from non-specificprotein binding. As demonstrated in this article, Cleanascite™ isthe only suitable reagent that can highly differentiate thelipid-bound protein from the non-lipid protein. This feature can beapplied to any investigation whereby the free and lipid-bound statesneed to be measured in the context of understanding disease or in thequest for biomarkers.” states Swapan Roy, Ph.D., President andFounder of Biotech Support Group.

Downloadwhitepaper entitled “Cleanascite™- Lipid Removal and Cell Response Applications”,visit:

Formore information visit: Cleanascite™Lipid Removal Reagent and Clarification,at
http://www.biotechsupportgroup.com/Cleanascite-Lipid-Removal-Reagent-p/x2555.htm

Keywords:Lipiddepletion, Cleanascite™, VitaminD Binding Protein; high density lipoprotein; psoriasis; coronaryartery disease

AboutBiotech Support Group LLC

Convergingwith cultural and technological disruptions forthcoming inhealthcare, Biotech Support Group develops methods for cost effectiveand efficient sample prep essential for these expanding markets.Following a tiered business strategy, the company continues itsgrowth in the consumable research products area supporting therapidly expanding installation of LC-MS instrument and computationalinfrastructure. Forthis market, key products include: AlbuVoid™ and AlbuSorb™ PLUSforalbumin & IgG depletion, Cleanascite™for lipid adsorption, HemogloBind™ and HemoVoid™ for hemoglobinremoval, and NRicher™ for targeted proteomics and family specificproteome enrichment.For more information, go tohttp://www.biotechsupportgroup.com.

ForBusiness Development,contact:MatthewKuruc 732-274-2866, [email protected]