Recombinant Human PMP2 Protein (N-6His)

Name: Recombinant Human PMP2 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0364NP
Availability: InStock

BL-0364NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Myelin P2 Protein is produced by our E.coli expression system and the target gene encoding Met1-Val132 is expressed with a 6His tag at the N-terminus.
Accession	P02689
Synonym	Myelin P2 Protein; Peripheral Myelin Protein 2; PMP2
Gene Background	Myelin P2 Protein (PMP2) is a cytoplasmic protein which belongs to the Fatty-acid binding protein (FABP) family of calycin superfamily. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. PMP2 is found in peripheral nerve myelin and spinal cord myelin, the oligodendrocytes and Schwann cells, respectively. PMP2 may be involved in lipid transport protein in Schwann cells. It may decrease the inhibitory effect of T suppressors in the culture of immune lymph node cells.
Molecular Mass	17.07 KDa
Apmol Mass	14-20 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Citrate, 10% Trehalose, 100mM NaCl, 0.05% Tween 80, pH 4.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	May play a role in lipid transport protein in Schwann cells. May bind cholesterol.
Subcellular Location	Cytoplasm.
Protein Families	Calycin superfamily, Fatty-acid binding protein (FABP) family
Database References	HGNC: 9117 OMIM: 170715 KEGG: hsa:5375 STRING: 9606.ENSP00000256103 UniGene: Hs.571512

Gene Functions References

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. PMID: 29940944
SH3TC2, PMP2, and BSCL2 pathogenic variants might be rare in Chinese Charcot-Marie-Tooth (CMT) patients. PMID: 29336362
Our genetic and clinical findings in these kindred demonstrate that dominant PMP2 mutations cause Charcot-Marie- Tooth disease type 1. PMID: 27009151
A fully deuterated sample of myelin P2 protein was produced identifying the neutron crystal structure. PMID: 26527266
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. PMID: 26828946
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. PMID: 24419389
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 PMID: 20421974

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.