OMG Human

Oligodendrocyte Myelin Glycoprotein Recombinant Human
Cat. No.
BT14809
Source
Sf9, Baculovirus cells.
Synonyms
Oligodendrocyte-myelin glycoprotein, OMG, OMGP.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

OMG Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (25-418) and having a molecular mass of 45.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-100kDa).
OMG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Oligodendrocyte-myelin glycoprotein (OMG) is a cell membrane protein found on the surface of oligodendrocytes and specific neurons, such as Purkinje cells and pyramidal cells. OMG plays a role in inhibiting neurite outgrowth through its interaction with the Nogo receptor and p75 neurotrophin receptor complex.
Description
Recombinant human OMG protein, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It consists of 401 amino acids (residues 25-418), with an 8-amino acid His-tag at the C-terminus. The molecular weight of the protein is 45.4 kDa, but it appears as a band at approximately 50-100 kDa on SDS-PAGE due to glycosylation. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
The product is a clear solution that has been sterilized by filtration.
Formulation
The OMG protein is supplied in a solution at a concentration of 0.5 mg/ml. The solution contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the product frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of the OMG protein is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
Oligodendrocyte-myelin glycoprotein, OMG, OMGP.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
ICPLQCICTE RHRHVDCSGR NLSTLPSGLQ ENIIHLNLSY NHFTDLHNQL TQYTNLRTLD ISNNRLESLP AHLPRSLWNM SAANNNIKLL DKSDTAYQWN LKYLDVSKNM LEKVVLIKNT LRSLEVLNLS SNKLWTVPTN MPSKLHIVDL SNNSLTQILP GTLINLTNLT HLYLHNNKFT FIPDQSFDQL FQLQEITLYN NRWSCDHKQN ITYLLKWMME TKAHVIGTPC STQISSLKEH NMYPTPSGFT SSLFTVSGMQ TVDTINSLSV VTQPKVTKIP KQYRTKETTF GATLSKDTTF TSTDKAFVPY PEDTSTETIN SHEAAAATLT IHLQDGMVTN TSLTSSTKSS PTPMTLSITS GMPNNFSEMP QQSTTLNLWR EETTTNVKTP LPSVEHHHHH H.

Product Science Overview

Importance in Research and Medicine

MOG is a significant target in the study of inflammatory demyelinating diseases such as multiple sclerosis (MS) and MOG antibody-associated disease (MOGAD). The presence of MOG antibodies (Abs) has been linked to various CNS disorders, including acute disseminated encephalomyelitis (ADEM), neuromyelitis optica spectrum disorders (NMOSD), and optic neuritis (ON) . These antibodies can be transient in some diseases, like ADEM, or persistent in others, such as NMOSD and recurrent ON.

Recombinant Human MOG (rhMOG)

Recombinant human MOG (rhMOG) is produced using genetic engineering techniques to express the MOG protein in a host system, such as bacteria. This recombinant protein is used in research to study the immune response in demyelinating diseases. One of the challenges in producing rhMOG has been its insolubility when overexpressed in bacterial cells, requiring inefficient denaturation and refolding steps .

Recent advancements have led to the development of high-yield production methods for soluble rhMOG using SHuffle cells, a commercially available E. coli strain engineered to facilitate disulfide bond formation in the cytoplasm . This method simplifies the production process and yields a well-folded, homogeneous monomeric protein that can be used in various research applications.

Applications in Experimental Autoimmune Encephalomyelitis (EAE)

Experimental autoimmune encephalomyelitis (EAE) is a widely used animal model for studying CNS autoimmune demyelinating diseases. Immunization with the extracellular domain of rhMOG, which contains pathogenic antibody and T cell epitopes, induces B cell-dependent EAE in mice . This model helps researchers understand the mechanisms of disease and test potential therapeutic interventions.

Clinical Relevance

The detection of MOG Abs in patients has clinical implications for diagnosing and managing various demyelinating diseases. Improved detection methods using cell-based assays with recombinant full-length, conformationally intact MOG have revealed that MOG Abs can be found in a subset of patients with different CNS disorders . Understanding the role of MOG Abs in these diseases can help in developing targeted therapies and improving patient outcomes.

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