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
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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.
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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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