PMP2 / FABP8 Protein (His Tag)

Myelin P2 ( PMP2 / FABP8 ) Protein

PMP2 / FABP8 Protein Product Information

• Synonym: PMP2, FABP8, M-FABP, MP2, P2
• Protein Construction: A DNA sequence encoding the human PMP2 ( NP_002668.1 ) ( Ser 2 - Val 132 ) was expressed, with a polyhistide tag at the N-terminus
• Source: Human
• Expression Host: E. coli

PMP2 / FABP8 Protein QC Testing

• Purity: > 97 % as determined by SDS-PAGE
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met 1
• Molecular Mass: The recombinant human PMP2 consisting of 138 amino acids and migrates as an approximately16 kDa band in SDS-PAGE under reducing conditions as predicted
• Formulation: Lyophilized from sterile PBS , pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

• SDS-PAGE: PMP2 protein

PMP2 / FABP8 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

PMP2 / FABP8 Protein Description

Myelin P2 protein, also known as PMP2, is a cytosolic protein found primarily in peripheral nerves. It Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. It is similar in amino acid sequence and tertiary structure to fatty acid binding proteins found in the liver, adipocytes, and intestine, its expression is limited to the nervous system. PMP2 is detected only in myelin-producing cells of the central and peripheral nervous systems, the oligodendrocytes and Schwann cells, respectively. PMP2 may play a role in lipid transport protein in Schwann cells. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

References

1. Hayasaka, K. et al., 1993, Genomics. 18 (2): 244-8.
2. Polverini, E. et al., 2006, J Struct Biol. 153 (3): 253-63.
3. Gould,R.M. et al., 2008, Neuron Glia Biol. 4 (2):137-52.