IL-10 Protein, Feline

IL-10 Protein, a key immune regulator, mitigates inflammation by binding to its receptor (IL10RA/IL10RB), activating JAK1 and STAT2, leading to STAT3-mediated anti-inflammatory gene expression. IL-10 targets APCs, reducing pro-inflammatory cytokines and hindering antigen presentation. It controls macrophage inflammation through metabolic reprogramming. Existing as a homodimer, IL-10 interacts with IL10RA/IL10RB. IL-10 Protein, Feline is the recombinant IL-10 protein, expressed by E. coli , with tag free. The total length of IL-10 Protein, Feline is 160 a.a., with molecular weight of ~19 kDa.

IL-10, a major immune regulatory cytokine, exerts profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL-10 binds to its heterotetrameric receptor, comprised of IL10RA and IL10RB, leading to JAK1 and STAT2-mediated phosphorylation of STAT3. Subsequently, phosphorylated STAT3 translocates to the nucleus, where it drives the expression of anti-inflammatory mediators. IL-10 specifically targets antigen-presenting cells (APCs) such as macrophages and monocytes, inhibiting their release of pro-inflammatory cytokines, including GM-CSF, G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8, and TNF-alpha. Additionally, IL-10 interferes with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation. Moreover, IL-10 controls the inflammatory response of macrophages by reprogramming essential metabolic pathways, including mTOR signaling. IL-10 exists as a homodimer and interacts with IL10RA and IL10RB.

Others

E. coli

Tag Free

P55029 (S19-I178)

493683  [NCBI]

Approximately 19 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.