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Human RGMa Protein 4712

$270.00$900.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Cys48-Gly422
SKU: 4712parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

Q96B86

express system

HEK293

product tag

C-His-Avi

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Repulsive guidance molecule (RGM) is a glycosylphosphatidylinositol (GPI)-anchored glycoprotein that has diverse functions in the developing and pathological central nervous system (CNS). The binding of RGM to its receptor neogenin regulates axon guidance, neuronal differentiation, and survival during the development of the CNS. RGMa induces T cell activation in experimental autoimmune encephalomyelitis (EAE), which is the animal model of multiple sclerosis (MS).  RGM is expressed in pathogenic Th17 cells and induces neurodegeneration by binding to neogenin.

molecular weight

The protein has a predicted MW of 44.5 kDa. Due to glycosylation, the protein migrates to 45-48 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human RGMa Protein 4712

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Repulsive guidance molecule (RGM) is a glycosylphosphatidylinositol (GPI)-anchored glycoprotein that has diverse functions in the developing and pathological central nervous system (CNS). The binding of RGM to its receptor neogenin regulates axon guidance, neuronal differentiation, and survival during the development of the CNS. RGMa induces T cell activation in experimental autoimmune encephalomyelitis (EAE), which is the animal model of multiple sclerosis (MS).  RGM is expressed in pathogenic Th17 cells and induces neurodegeneration by binding to neogenin.
Protein names
Repulsive guidance molecule A (RGM domain family member A)
Gene names
RGMA,RGMA RGM
Protein family
Repulsive guidance molecule (RGM) family
Mass
9606Da
Function
FUNCTION: Member of the repulsive guidance molecule (RGM) family that performs several functions in the developing and adult nervous system. Regulates cephalic neural tube closure, inhibits neurite outgrowth and cortical neuron branching, and the formation of mature synapses. Binding to its receptor NEO1/neogenin induces activation of RHOA-ROCK1/Rho-kinase signaling pathway through UNC5B-ARHGEF12/LARG-PTK2/FAK1 cascade, leading to collapse of the neuronal growth cone and neurite outgrowth inhibition. Furthermore, RGMA binding to NEO1/neogenin leads to HRAS inactivation by influencing HRAS-PTK2/FAK1-AKT1 pathway. It also functions as a bone morphogenetic protein (BMP) coreceptor that may signal through SMAD1, SMAD5, and SMAD8. {ECO:0000269|PubMed:19273616, ECO:0000269|PubMed:19458235}.
Subellular location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Structure
SUBUNIT: Interacts with NEO1, BMP2 and BMP4. {ECO:0000250}.
Post-translational modification
PTM: Autocatalytically cleaved at low pH; the two chains remain linked via two disulfide bonds. {ECO:0000250}.
Target Relevance information above includes information from UniProt accession : Q96B86
The UniProt Consortium

Data

ELISA with Human RGMa Protein
Immobilized Human RGMa, His Tag at 5µg/ml (100µl/Well) on the plate. Dose response curve for Human Neogenin, hFc Tag with the EC50 of 0.17µg/ml determined by ELISA.
HPLC of Human RGMa Protein
The purity of Human RGMa is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human RGMa Protein
Human RGMa on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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Protocols

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