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May play a role in lipid transport protein in Schwann cells. Additionally we are shipping PMP2 Proteins (22) and PMP2 Kits (18) and many more products for this protein.
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The structural characterization of the F57A mutant of P2 which shows changes in the portal region and helix alpha2 and an unfolded status upon lipid bilayer binding. Further results suggest a central role for Phe57 in regulating the opening of the portal region in human P2, and the F57A mutation disturbs dynamic cross-correlation networks in the portal region of P2.
SH3TC2, PMP2, and BSCL2 pathogenic variants might be rare in Chinese Charcot-Marie-Tooth (CMT) patients.
Our genetic and clinical findings in these kindred demonstrate that dominant PMP2 mutations cause Charcot-Marie- Tooth disease type 1.
A fully deuterated sample of myelin P2 protein was produced identifying the neutron crystal structure.
This report might expand the genetic and clinical features of Charcot-Marie-Tooth disease and a further mechanism study will enhance our understanding of PMP2-associated peripheral neuropathy.
The structure of human P2 refined at the ultrahigh resolution of 0.93 A allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network.
the structure and function of the P2 protein from human myelin, which is able to bind both monomeric lipids inside its cavity and membrane surfaces
Oleic, stearic, and palmitic fatty acids are associated with P2 myelin protein protein.
May play a role in lipid transport protein in Schwann cells. May bind cholesterol.
myelin P2 protein