Recombinant Human ERMAP Fc Chimera Protein, CF

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Measured by its ability to inhibit anti-CD3 antibody induced IL-2 secretion by human T cells. The ED50 for this effect is 0.75-7.5 μg/mL.
2 μg/lane of Recombinant Human ERMAP Fc Chimera (Catalog # 10645-ER) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human ERMAP Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit anti-CD3 antibody induced IL-2 or IFN-gamma secretion by human T cells. ED50 for this effect is 0.75-7.5 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human ERMAP protein
Human ERMAP
(His30-Ala155)
Accession # Q96PL5.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
His30 & Gly32
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.
Purity Statement
Antigen Affinity-purified
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
40 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
40-55 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, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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 ERMAP Fc Chimera Protein, CF

  • ERMAP
  • erythroblast membrane-associated protein (RD and SC blood groups)
  • erythroblast membrane-associated protein (Scianna blood group)
  • erythroblast membrane-associated protein
  • erythroid membrane-associated protein
  • hERMAP
  • MGC118810
  • MGC118811
  • PRO2801
  • Radin blood group (Rd)
  • Radin blood group antigen
  • Radin blood group
  • RD
  • RDMGC118812
  • SC
  • Scianna blood group (Sc)
  • Scianna blood group antigen
  • Scianna blood group
  • SCMGC118813

Background

Erythroid membrane-associated protein (ERMAP), also called Scianna blood group antigen, is a member of the butrophilin (BTN) and butrophilin-like (BTNL) family within the immunoglobulin superfamily. ERMAP consists of an extracellular domain (ECD) with one V-type Ig-like (IgV) fold, a transmembrane segment, and a cytoplasmic domain with a B30.2 motif (1).  Within the ECD, human ERMAP shares 33% and 31% amino acid sequence identity with mouse and rat ERMAP, respectively. Interestingly, human ERMAP contains a single IgV-like domain in the ECD, while mouse and rat ERMAP contain both an IgV-like and IgC-like domain. However, the absence of the IgC-like domain in human ERMAP does not seem to affect its functions (2, 3). ERMAP is an adhesion receptor molecule highly expressed in erythroid tissues, on the cell surface of resting and activated antigen-presenting cells (APCs) and in some tumor tissues (1, 4, 5). Fusion proteins (ERMAP-Ig) of both human and mouse ERMAP inhibit T cell functions in vitro and administration of the fusion protein ameliorates autoimmune diseases, including experimental autoimmune encephalomyelitis and type 1 diabetes, in mice (5). ERMAP acts as a novel inhibitory molecule for T cells and macrophages (5).
  1. Xu, H. et al. (2001) Genomics 76:2.
  2. Compte, E.W. et al. (2004) Eur. J. Immunol. 34:2089.
  3. Su, Y.Y. et al. (2001) Blood Cell Mol. Dis. 27:938
  4. Abeler-Dorner, L. et al. (2012) Trends Immunol. 33:34.
  5. Su, M. et al. (2020) Cell. Mol. Immunol. doi: 10.1038/s41423-020-0494-8.

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