Recombinant Rat Fc gamma RI/CD64 Protein, CF

When Recombinant Rat Fc gamma RI/CD64(Catalog # 9558‑FC) is immobilized at 1 μg/mL, 100 μL/well, BiotinylatedRat IgG binds with an ED50 of 0.075‑0.35 μg/mL.

• Reactivity: Rt
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Rat Fc gamma RI/CD64 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Rat Fc gamma RI/CD64 is immobilized at 1 μg/mL, 100 μL/well, it binds Biotinylated Rat IgG. The concentration of Biotinylated Rat IgG that produces 50% of the optimal binding response is 0.075-0.35 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived rat Fc gamma RI/CD64 protein
  Gln16-Pro285, with a C-terminal 6-His tag
• Accession #: NP_001094306
• N-terminal Sequence: Thr21 observed & Gln16 inferred from enzymatic pyroglutamate treatment revealing Val17
• 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: 31 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: 36-48 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 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS and Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 1 mg/mL in PBS.

Notes

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

Alternate Names for Recombinant Rat Fc gamma RI/CD64 Protein, CF

• CD64 antigen
• CD64
• CD64a
• Fc fragment of IgG, high affinity Ia, receptor (CD64)
• Fc gamma RI
• FCG1
• Fc-gamma receptor I B2
• Fc-gamma RI
• Fc-gamma RIA
• FcgammaRIa
• FCGR1
• FcgRI
• FcgRIA
• FCRI
• FcRIA
• FLJ18345
• high affinity Ia, receptor for (CD64)
• high affinity immunoglobulin gamma Fc receptor I
• IgG Fc receptor I

Background

Receptors for the Fc region of IgG (Fc gamma  Rs) are members of the Ig superfamily that function in the activation or inhibition of immune responses such as degranulation, phagocytosis, cytokine release, and B cell proliferation. There are three classes of Fc gamma  Rs, based on close relationships in their extracellular domains: Fc gamma  RI/CD64, Fc gamma RII/CD32, and Fc gamma  RIII/CD16. Each group may be encoded by multiple genes and exists in different isoforms depending on species and cell type (1-3). The CD64 proteins are high affinity receptors (~10^-8-10^-9 M) that are capable of binding monomeric IgG, whereas the CD16 and CD32 proteins bind IgG with lower affinities (~10^-6-10^-7 M) (4, 5). The high affinity of IgG by Fc gamma  RI permits the triggering of effector responses at low IgG concentrations typical of early immune response (6). The mature protein from this family consists of an extracellular domain (ECD), a transmembrane segment, and a cytoplasmic domain. Within the ECD, rat Fcɣ RI shares 78% and 64% amino acid sequence identity with mouse and human Fc gamma RI, respectively. Fc gamma RI is expressed constitutively on monocytes and macrophages and can be induced on neutrophils and eosinophils. Its expression is up-regulated during bacterial infections and sepsis (1, 5).

1. Van de Winkel, J. and P. Capes (1993) Immunol. Today. 14:215.
2. Raghaven, M. and P. Bjorkman (1996) Annu. Rev. Cell Dev. Biol. 12:181.
3. Ravetch, J. and S. Bolland (2001) Annu. Rev. Immunol. 19:275.
4. Chenoweth, A.M et al. (2015) Immunol. Rev. 268:175.
5. Takai, T. (2002) Nature Rev. Immunol. 2:580.
6. Raghaven, M. and P. Bjorkman (1996) Annu. Rev. Cell Dev. Biol. 12:181.

Bioinformatics

• Uniprot:
  • NP_001094306()