Recombinant Canine IL11RA protein(Met1-Leu363)

• Cat.No.: IL11RA-1268C
• Product Overview: Recombinant Canine IL11RA (XP_538710.4) (Met1-Leu363) was expressed in HEK293 with six amino acids (LEVLFQ) at the C-terminus.

Specification

• Source: HEK293
• Species: Canine
• Tag: Non
• Protein length: Met1-Leu363
• Form: Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant Canine IL11RA is a disulfide-linked homodimer. The reduced monomer comprises 348 amino acids and has a predicted molecular mass of 37.8 kDa. The apparent molecular mass of the protein is approximately 43-47 kDa in SDS-PAGE under reducing conditions.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Purity: > 90 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.
• Official Symbol: IL11RA

Gene Information

• Official Symbol: IL11RA

Reviews

02/15/2021

High affinity binding.

09/05/2020

Stable in solution.

02/20/2017

Effective in hematopoiesis studies.

Q&As

Can you explain how phosphoproteomics and mass spectrometry shed light on IL11RA-mediated signaling cascades and post-translational modifications?

Phosphoproteomics and mass spectrometry reveal IL11RA-related signaling pathways.

How are flow cytometry and fluorescence-activated cell sorting (FACS) employed to analyze IL11RA expression on different cell populations?

Flow cytometry and FACS analyze IL11RA expression on different cell types.

Could you elaborate on how X-ray crystallography and cryo-electron microscopy contribute to understanding the three-dimensional structure of IL11RA?

X-ray crystallography and cryo-EM reveal the three-dimensional structure of IL11RA.

What insights have gene expression profiling and RNA sequencing provided regarding IL11RA-related molecular pathways and networks?

Gene expression profiling and RNA sequencing unveil IL11RA-associated molecular networks.

How do techniques like co-immunoprecipitation and pull-down assays validate IL11RA's interactions with IL11 and other signaling partners?

Co-immunoprecipitation and pull-down assays confirm IL11RA interactions with IL11 and other partners.

What role does site-directed mutagenesis play in identifying IL11RA residues critical for IL11 binding and downstream signaling activation?

Site-directed mutagenesis identifies IL11RA residues crucial for binding and signaling.

How are animal models like transgenic mice and tissue-specific knockouts utilized to study the in vivo roles of IL11RA in development and disease?

Transgenic mice and knockouts study IL11RA's roles in development and disease.

Can you explain the experimental strategies used to characterize IL11RA isoforms and their differential roles in IL11 signaling?

Experimental strategies characterize IL11RA isoforms and their distinct roles in IL11 signaling.

How are biophysical techniques such as isothermal titration calorimetry and surface plasmon resonance used to determine IL11RA's binding affinities and kinetics?

Isothermal titration calorimetry and surface plasmon resonance measure IL11RA binding properties.

What methods like CRISPR-Cas9 knockout and RNA interference help elucidate the functional significance of IL11RA in specific biological contexts?

CRISPR-Cas9 knockout and RNA interference reveal IL11RA's functions in specific contexts.