Human IL-11 R alpha Antibody Summary
Ser24-Val363
Accession # Q14626
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of Human, Mouse, and Rat IL‑11 R alpha by Western Blot. Western blot shows lysates of human skeletal muscle tissue, mouse skeletal muscle tissue, and rat skeletal muslce tissue. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human IL-11 Ra Monoclonal Antibody (Catalog # MAB19771) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for IL-11 Ra at approximately 45-49 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Human IL‑11 R alpha by Simple WesternTM. Simple Western lane view shows lysates of human skeletal muscle, loaded at 0.2 mg/mL. A specific band was detected for IL‑11 R alpha at approximately 49 kDa (as indicated) using 50 µg/mL of Mouse Anti-Human IL‑11 R alpha Monoclonal Antibody (Catalog # MAB19771). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-11 R alpha
Interleukin-11 receptor alpha (IL-11 R alpha ) is a 49 kDa type I transmembrane member of the gp130 subfamily of the hematopoietic cytokine receptor family (1-3). Mature human IL-11 R alpha consists of a 347 amino acid (aa) extracellular domain (ECD) that contains a C2 type Ig-like domain, two fibronectin type III domains, two potential glycosylation sites, and a WSxWS motif, followed by a 21 aa transmembrane region and a 31 aa cytoplasmic domain (4). Within the ECD, human IL-11 R alpha shares 84%, 82%, 90%, and 86% aa sequence identity with mouse, rat, equine, and bovine IL-11 R alpha, respectively. Alternative splicing generates an additional isoform that lacks the cytoplasmic domain (4). Upon low affinity binding to IL-11, IL-11 R alpha associates with gp130 to form a high affinity receptor complex (1, 3). gp130 also functions as a subunit in the receptors for Cardiotrophin-1, CNTF, IL-6, IL-27, IL-31, LIF, and Oncostatin M (5). IL-11 R alpha is widely expressed in adults, embryos, and embryonic stem cells (4, 6, 7). Deletion of IL-11 R alpha in female mice causes faulty decidualization, lack of decidual NK cells, and infertility (8-10). IL-11 is anti-apoptotic for oligodendrocytes, and lack of IL-11 R alpha increases the severity of experimental autoimmune encephalitis (11, 12). IL-11 R alpha is also anti-apoptotic for colonic epithelia, and increased IL-11 signaling may be a factor in inflammation-associated gastrointestinal cancer development (3, 13). IL-11 R alpha enhances osteoclast differentiation and bone remodeling but inhibits adipocyte differentiation (1, 2). Recombinant soluble IL-11 R alpha confers IL-11 responsiveness to cells expressing gp130, while in cells expressing transmembrane IL-11 R alpha and gp130, soluble IL-11 R alpha acts as an IL-11 antagonist (14-16).
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