AIMP1 Recombinant Protein His Tag Lyophilized from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in PBS, pH7.4 with a purity of >95% as determined by SDS-PAGE.

Endotoxin level is less than 1.0 EU per ug by the LAL method..

More Details:

• Species: Bacteria-Derived
• Target: AIMP1
• Purity: >95% as determined by SDS-PAGE.
  
  Endotoxin level is less than 1.0 EU per ug by the LAL method.
• Source: E. coli
• Storage Conditions: Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles.

Additional Information:

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (AIMP1) is also known as multisynthase complex auxiliary component p43 and endothelial monocyte-activating polypeptide II (EMAP-II). AIMP1 is a cytokine that may be induced by apoptosis and is also released from professional antigen-presenting cells such as dendritic cells. The release of AIMP1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 binds tRNA and stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. This protein possesses inflammatory cytokine activity. Also, AIMP1 negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation.

This recombinant protein can be used for WB. For research use only.. At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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