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Human AIMP1 / EMAP2 / SCYE1 Protein  pdf  pdf  pdf

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Human AIMP1, His Tag (EM2-H5142) is expressed from E.coli cells. It contains AA Ala 2 - Lys 312 (Accession # AAH14051).

Predicted N-terminus: Met

Molecular Characterization

AIMP1(Ala 2 - Lys 312)AAH14051

This protein carries a polyhistidine tag at the N-terminus.

The protein has a calculated MW of 35.2 kDa. The protein migrates as 36 kDa under reducing (R) condition (SDS-PAGE).


Less than 1.0 EU per μg by the LAL method.


>95% as determined by SDS-PAGE.


Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

Contact us for customized product form or formulation.


Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.


For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

No activity loss is observed after storage at:

  1. 4-8°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.


Human AIMP1, His Tag (Cat. No. EM2-H5142) SDS-PAGE gel

Human AIMP1, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.



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.


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