Recombinant Human Oligodendrocyte myelin glyco / OMGPprotein Protein (aa 1-416, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3586

Recombinant Human Oligodendrocyte myelin glyco / OMGPprotein Protein (aa 1-416, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3586
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Product Overview

Tag His
Host Species Human
Accession P23515
Synonym OMGP
Background Oligodendrocyte-myelin glycoprotein, also known as OMG and OMGP, is a cell membrane protein which contains eightLRR (leucine-rich) repeats. OMG / OMGP is a glycosylphosphatidylinositol-anchored protein expressed by neurons and oligodendrocytes in the central nervous system (CNS). OMG / OMGP is a cell adhesion molecule contributing to the interactive process required for myelination in the central nervous system. OMG / OMGP play roles in both the developing and adult central nervous system. OMG / OMGP participats in growth cone collapse and inhibition of neurite outgrowth through its interaction with NgR, the receptor for Nogo. This function requires its leucine-rich repeat domain, a highly conserved region in OMgp during mammal evolution. OMG / OMGP leucine-rich repeat domain is also implicated in the inhibition of cell proliferation. OMG / OMGP may also be involved in the formation and maintenance of myelin sheaths. Cell proliferation, neuronal sprouting and myelination are crucial processes involved in brain development and regeneration after injury.
Description A DNA sequence encoding the mature form of human OMGP (P23515-1) (Met 1-Pro 416) without the pro peptide was expressed, fused with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Ile 25
AA Sequence Met 1-Pro 416
Molecular Weight The secreted recombinant human OMGP comprises 403 a.a. and has a predicted molecular mass of 46 kDa. The apparent molecular mass of rh OMGP is approximately 120-130 kDa in SDS-PAGE under reducing conditions due to high glycosylation.
Purity >97% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by the ability of the immobilized protein to support the adhesion of C6 Rat brain glial cells. Immobilized OMG (0.8 ug/ml, 100 ul/well) will mediate >15% C6 cell adhesion.
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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.

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