Recombinant Human CD117/c-kit Fc Chimera Protein, CF Summary
|Human SCFR |
Accession # P10721.1
|IEGRMD||Human IgG1 Fc|
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Recombinant Human CD117/c-kit Fc Chimera Protein (Catalog # 10961-SR) inhibits SCF-dependent proliferation of TF‑1 human erythroleukemic cells. The ED50 for this effect is 30.0-180 ng/mL.
2 μg/lane of Recombinant Human CD117/c-kit Fc Chimera Protein (Catalog # 10961-SR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 100-120 kDa and 200-240 kDa, respectively.
Stem cell factor receptor (SCFR), also known as c-Kit and CD117, is a type III receptor tyrosine kinase that acts as the receptor for the cytokine SCF. Human SCFR is expressed in embryonic stem cells and is involved in regulation of cell survival and proliferation, hematopoiesis, gametogenesis, and melanogenesis (1-3). Mature human SCFR consists of an extracellular domain (ECD) with five tandem immunoglobulin-like domains, a single transmembrane segment, and a cytoplasmic region with a split tyrosine kinase domain. Within the ECD, human SCFR shares 73% and 76% amino acid sequence identity with mouse and rat SCFR, respectively. Several SCFR isoforms, produced by alternative mRNA splicing, have been identified in humans and can be characterized by the presence or absence of a tetrapeptide sequence (GNNK) in the juxtamembrane region of the ECD (4, 5). Binding of SCFR to SCF triggers receptor dimerization and activates downstream signaling (6). SCF is a primary growth and activation factor for mast cells and eosinophils and SCFR expression on mast cells enables them to infiltrate SCF‑secreting tumors where they promote tumor growth and induce local immune suppression (7, 8). SCFR is up regulated on dendritic cells by Th2- or Th17-biasing stimuli, and it is required for subsequent dendritic cell induction of Th2 and Th17 responses (9). SCFR protects vascular smooth muscle cells from apoptosis and assists in the recovery of cardiac function following myocardial infarction (10, 11). Mutations or deletions of SCFR cause a wide variety of malignancies as well as pigmentation disorders and sterility (12).
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