IL-4R/CD124 (Tyr497) polyclonal Antibody | AP0210

IL-4R/CD124 (Tyr497) polyclonal Antibody | AP0210 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Application: WB

Application Range: WB: 1:1000~1:2000

Background: The IL-2 receptor is a multicomponent complex consisting of three subunits, α,β and γ, each of which is required for high affinity binding of IL-2. The α chainfunctions primarily in binding IL-2, whereas the β and γ chains contribute toIL-2 binding and are essential to IL-2-induced activation of signaling pathwaysleading to T cell growth. Both IL-4R and IL-7R were initially described as single chain, high-affinity ligand-binding cytokine receptors. However, it is nowwell established that the IL-2Rγ chain functions as a second subunit of thehigh affinity IL-4R and IL-7R receptors. Consequently, the originally describedsubunits of these latter receptors are now referred to as IL-4Rα and IL-7Rα,respectively, while the common subunit is referred to as γc. Although the common γ chain enhances ligand binding in these three cytokine receptors, ithas no capacity to bind these ligands on its own. There is evidence that theγc chain is also a subunit of IL-13R.

Storage & Stability: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Specificity: IL-4R/CD124 (Tyr497) polyclonal Antibody detects endogenous levels of HIST1H3A protein.

Molecular Weight: ~ 85 kDa

Note: For research use only, not for use in diagnostic procedure.

Alternative Names: Interleukin-4 receptor subunit alpha; IL-4 receptor subunit alpha; IL-4R subunit alpha; IL-4R-alpha; IL-4RA; CD_antigen: CD124; Soluble IL-4 receptor subunit alpha; Soluble IL-4R-alpha; sIL4Ralpha/prot; IL-4-binding protein; IL4-BP; IL4R; 582J2.1

Immunogen: Synthetic peptide, corresponding to Human IL-4R/CD124 (Tyr497) .

Conjugate: Unconjugated

Modification: Unmodification

Purification & Purity: The Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Pathway: