Recombinant Human Repulsive Guidance Molecule A Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-7719P

Recombinant Human Repulsive Guidance Molecule A Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-7719P
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Product Overview

Host Species Human
Accession Q96B86
Synonym Repulsive guidance molecule A RGM RGM domain family member A RGMA RGMA_HUMAN
Description Recombinant Human Repulsive Guidance Molecule A Protein (His tag) was expressed in E.coli. It is a Protein fragment
Source E.coli
AA Sequence MNHKVHHHHHHMPHLRTFTDRFQTCKVQGAWPLIDNNYLNVQVTNTPVLP GSAATATSKLTIIFKNFQECVDQKVYQAEMDELPAAFVDGSKNGGDKHGA NSLKITEKVSGQHVEIQAKYIGTTIVVRQVGRYLTFAVRMPEEVVNAVED WDSQGLYLCLRGCPLNQQIDFQAFHTNAEGTGARRLAAASPAPTAPETFP YETAVAKCKEKLPVEDLYYQACVFDLLTTGDVNFTLAAYYALEDVKMLHS NKDKLHLYER TRDLPG
Molecular Weight 30 kDa including tags
Purity Greater than 95% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on Dry Ice. Store at -80°C.

Target Details

Target 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.
Subcellular Location Cell membrane; Lipid-anchor, GPI-anchor.
Protein Families Repulsive guidance molecule (RGM) family
Database References

Gene Functions References

  1. Dysregulation of RGMa plays an important role in the pathology of Parkinson's disease. PMID: 28842419
  2. Thus, we conclude that RGMa inhibits angiogenesis in vitro and in vivo suggesting that its manipulation would be an efficient therapeutic strategy for pro-angiogenic conditions. PMID: 26721439
  3. RGMa expression and promoter methylation status are closely related to colorectal cancer genesis and progression. PMID: 22367090
  4. identification of neogenin-binding site on the repulsive guidance molecule A PMID: 22396795
  5. The expression of RGMA, RGMB and RGMC was evident in most examined prostate cancer cell lines, and also in the prostate cancer tissues PMID: 22076499
  6. Reduced expression of RGMA in breast cancer was associated with breast cancer. PMID: 21617229
  7. The full-length signal peptides of RGMa is functional and furthermore that the C-domains are sufficient and essential for ER targeting, whereas the N-domains are dispensable. Thus, the N-domains are available for additional functions. PMID: 21183991
  8. RGM-A is a unique endogenous inhibitor of leukocyte chemotaxis that limits inflammatory leukocyte traffic PMID: 21467223
  9. Following central nervous system injury, RGM, a novel, potent axonal growth inhibitor, is present in axonal growth impediments: the mature myelin, choroid plexus, and components of the developing scar. PMID: 16216939
  10. RGMa facilitates the use of ActRIIA by endogenous BMP2 and BMP4 ligands that otherwise prefer signaling via BMPRII and increased utilization of ActRIIA leads to generation of an enhanced BMP signal PMID: 17472960
  11. detected a homozygous deletion of chromosomal region 15q26.2 in the cell line HDLM2 encompasing RGMA and CHD2 PMID: 17606441
  12. this study, we show that Unc5B, a member of the netrin receptor family, interacts with neogenin as a coreceptor for RGMa. PMID: 19273616
  13. Frequent inactivation of axon guidance molecule RGMA in human colon cancer through genetic and epigenetic mechanisms. PMID: 19303019

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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