Recombinant Human CRACC/SLAMF7 Fc Chimera Protein, CF

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2 μg/lane of Recombinant Human CRACC/SLAMF7 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 65-75 kDa and 130-150 kDa, ...read more
Recombinant Human CRACC/SLAMF7 Fc Chimera (Catalog # 1906-SF) inhibits anti-CD3 antibody induced IFN-gamma secretion by human peripheral blood mononuclear cells. The ED50 for this effect is 2-10 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human CRACC/SLAMF7 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit anti-CD3 antibody induced IFN-gamma secretion by human peripheral blood mononuclear cells (PBMC). The ED50 for this effect is 1-6 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human CRACC/SLAMF7 protein
Human SLAMF7
(Ser23-Met226)
Accession # Q9NQ25
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Ser23
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

Theoretical MW
49 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
65-75 kDa, 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 °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 100 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 CRACC/SLAMF7 Fc Chimera Protein, CF

  • 19A
  • CD2 subset 1
  • CD2-like receptor activating cytotoxic cells
  • CD319 antigen
  • CD319
  • CRACC
  • CRACCCD2-like receptor-activating cytotoxic cells
  • CS119A24 protein
  • Membrane protein FOAP-12
  • novel LY9 (lymphocyte antigen 9) like protein
  • Novel Ly9
  • Protein 19A
  • SLAM family member 7
  • SLAMF7

Background

CD2-like receptor activating cytotoxic cells (CRACC), also known as CS1, novel Ly9, SLAMF7, and CD319, is a 65-75 kDa type I transmembrane glycoprotein in the SLAM subgroup of the CD2 family (1). Mature human CRACC consists of a 204 amino acid (aa) extracellular domain (ECD) with one Ig-like V-set domain and one Ig-like C2-set domain, a 21 aa transmembrane segment, and an 88 aa cytoplasmic domain with one immunoreceptor tyrosine-based switch motif (ITSM) (2, 3). Within the ECD, human CRACC shares 54% and 52% aa sequence identity with mouse and rat CRACC, respectively. There are seven known isoforms of CRACC which are distinguished by deletions and/or substitutions in both their ECD and cytoplasmic domains. CRACC is expressed on the surface of NK cells, CD8+ T cells, activated B cells, and mature dendritic cells (4, 5). Its homophilic interaction induces NK, CTL, and B cell activation (4-7). In human NK cells, activated CRACC transmits signals following association with the adaptor protein EAT-2 (8).
  1. Veillette, A. (2006) Immunol. Rev. 214:22.
  2. Tovar, V. et al. (2002) Immunogenetics 54:394.
  3. Murphy, J.J. et al. (2002) Biochem. J. 361:431.
  4. Bouchon, A. et al. (2001) J. Immunol. 167:5517.
  5. Lee, J.K. et al. (2007) J. Immunol. 179:4672.
  6. Kumaresan, P.R. et al. (2002) Mol. Immunol. 39:1.
  7. Stark, S. and C. Watzl (2006) Int. Immunol. 18:241.
  8. Tassi, H. and M. Colonna (2005) J. Immunol. 175:7996.

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