Recombinant Human MDGA1 Fc Chimera Protein, CF

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When Recombinant Human MDGA1 Fc Chimera Protein (Catalog # 11368-MD) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human Neuroligin 2/NLGN2 (5645-NL) binds with an ED50 of 0.125-1.50 µg/mL.
2 μg/lane of Recombinant Human MDGA1 Fc Chimera Protein (Catalog # 11368-MD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human MDGA1 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human MDGA1 Fc Chimera (Catalog # 11368-MD) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human Neuroligin 2/NLGN2  (Catalog # 5645-NL) binds with an ED50 of 0.125-1.50 µg/mL.
Source
Human embryonic kidney cell, HEK293-derived human MDGA1 protein
Human MDGA1
(Gln19-Gly931)
Accession # Q8NFP4.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
No results obtained: Gln19 predicted
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
128 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
125-145 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human MDGA1 Fc Chimera Protein, CF

  • FLJ45018
  • GPIM
  • MAM domain containing glycosylphosphatidylinositol anchor 1
  • MAMDC3
  • MDGA1

Background

MDGA1 (MAM domain containing glycosylphosphatidylinositol anchor 1) is a 135‑140 kDa glycoprotein within the IgCAM superfamily of adhesion molecules (1‑3). MDGA1 is thought to mediate neuronal migration, neurite outgrowth, and cell-cell adhesion within the central and peripheral nervous system (1, 4‑8). Human MDGA1 precursor is a 955 amino acid (aa) protein that produces a 914 aa mature protein with six Ig-like domains, a fibronectin type III domain (aa 640-739), a MAM domain (aa 751-918), and a GPI anchor (aa 932) (1-3). Mature human MDGA1 shares 95%, 96%, and 98% aa sequence identity with mature mouse, rat, and canine MDGA1, respectively. Potential human variants of 973, 904 and 587 aa contain a 48 aa substitution for aa 936-955, a 58 aa substitution for aa 847-955, and a 51 aa substitution for aa 537-955, respectively. Human MDGA1 also shares 54% aa sequence identity with human MDGA2, and may also share some functional redundancy (1, 4). MDGA1 is mainly expressed on restricted populations of neurons in the central and peripheral nervous system, such as embryonic neurons destined for cortical layers 2/3, migrating basilar pontine neurons and D1 interneurons of the spinal cord (1, 5‑7). Deletion or down‑regulation of mouse MDGA1 slows radial migration of neurons, indicating a role for MDGA1 in radial migration of cortical neurons (4, 5). MAM and Ig-like domains are involved in heterophilic and homophilic adhesion (7, 8). MDGA1 expression is also reported on primary cells and cell lines from leukemias, lymphomas, and tumors of the lung, colon, uterus, stomach and breast (3).
  1. Litwack, E.D. et al. (2004) Mol. Cell. Neurosci. 25:263.
  2. Diaz-Lopez, A. et al. (2005) Exp. Cell Res. 307:91.
  3. De Juan, C. et al. (2002) Oncogene 21:3089.
  4. Ishikawa, T. et al. (2011) Dev. Dyn. 240:96.
  5. Takeuchi, A. and D.D.M. O'Leary (2006) J. Neurosci. 26:4460.
  6. Takeuchi, A. et al. (2007) Cereb Cortex. 17:1531.
  7. Fujimura, Y. et al. (2006) Brain Res. 1101:12.
  8. Diaz-Lopez, A. et al. (2011) Cancer Microenviron. 4:23.

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