LIFR Protein (C-Term, Extracellular Domain)

Catalog No. ABIN1684648

Product Details

Target: LIFR (Leukemia Inhibitory Factor Receptor alpha (LIFR))

Protein Type: Recombinant

Protein Characteristics: C-Term, Extracellular Domain

Origin: Mouse

Source: HEK-293T Cells

Specificity: Optimized DNA sequence encoding extracellular domain of mouse CD118 (LIFR) including a C-terminal 6His tag was expressed in HEK293 cells.

Characteristics: Recombinant CD118 (LIF receptor) is a monomer protein consisting of 796 amino acid residue subunits, due to glycosylation migrates as an approximately 110 kDa protein on SDS-PAGE.

Purity: > 90 %, as determined by SDS-PAGE and HPLC

Sterility: 0.2 μm filtered

Endotoxin Level: Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

Application Details

Restrictions: For Research Use only

Handling

Buffer: PBS solution, pH7.2

Handling Advice: Avoid repeated freeze/thaw cycles.

Storage: -20 °C

Storage Comment: The lyophilized protein is stable for at least years from date of receipt at -20 °C. Upon reconstitution, this cytokine can be stored in working aliquots at - 8 °C for one month, or at -20 °C for six months, with a carrier protein without detectable loss of activity.

Expiry Date: 12-24 months

Target Details

Target: LIFR (Leukemia Inhibitory Factor Receptor alpha (LIFR))

Alternative Name: CD118 (LIFR Products)

Synonyms: A230075M04Rik Protein, AW061234 Protein, LIF Protein, CD118 Protein, LIF-R Protein, SJS2 Protein, STWS Protein, SWS Protein, leukemia inhibitory factor receptor Protein, LIF receptor alpha Protein, leukemia inhibitory factor receptor alpha Protein, Lifr Protein, LOC397451 Protein, LIFR Protein

Background: IL-10 is produced by mouse Th2-cells following their stimulation by lectins. The main source for B-cell derived IL10 in mice are Ly1 B-cells that express CD5 (Ly1) and CD11. In humans IL10 is produced by activated CD8 (+) peripheral blood T-cells, by T-helper CD4 (+) T-cell clones after both antigen-specific and polyclonal activation, by B-cell lymphomas, and by monocytes following cell activation by bacterial lipopolysaccharides and mast cells. IL10 is a homodimeric protein with subunits having a length of 160 amino acids. Human Interleukin10 shows 73 % amino acid homology with mouse Interleukin-10. The murine IL-10 receptor has been cloned. This receptor is a protein of approximately 110 kDa that binds murine IL10 specifically. This receptor is structurally related to receptors for IFN. The CD nomenclature for this receptor is CDw210. IL10 inhibits the synthesis of a number of cytokines such as IFN-gamma, IL2 and TNF-beta in Th1 T-helper subpopulations of T-cells but not of Th2 T-helper cells. This activity is antagonized by IL4. The inhibitory effect on IFN-gamma production is indirect and appears to be the result of a suppression of IL12 synthesis by accessory cells. In the human system, IL10 is produced by, and down-regulates the function of Th1 and Th2 cells.

UniProt: P42702

Pathways: JAK-STAT Signaling, Growth Factor Binding