The diverse biological activities of G-CSF are initiated by the binding of G-CSF to a specific receptor (G-CSFR) that belongs to the cytokine/hematopoietic receptor superfamily. In contrast to the majority of hematopoietic receptors that are activated through the formation of heteromeric complexes composed of å, ß and sometimes g subunits, G-CSFR proteins are believed to form homodimeric complexes upon ligand binding. Four distinct alternative splice variants of G-CSFR have been described, one of which exists as a soluble receptor protein. Although G-CSFR lacks consensus motifs in its cytoplasmic domains that are characteristic of kinase activities, certain sequences have been identified that are conserved among several members of the cytokine receptor superfamily. For example, the carboxy terminal regions of G-CSFR contain a domain, designated box 3, that is only shared with the IL-6R subunit, gp130.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of G-CSFR of mouse, rat and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 25-200 mapping near the N-terminus of G-CSFR of human origin
Tissue Specificity
epitope corresponding to amino acids 25-200 mapping near the N-terminus of G-CSFR of human origin