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Human AIMP1 / EMAP2 / SCYE1 Protein  pdf  pdf  pdf


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Synonym

AIMP1, EMAP2, EMAPII, HLD3, SCYE1, p43, EMAP-2, EMAP-II, AIMP-1

Source

Human AIMP1 / EMAP2 / SCYE1 Protein (Human AIMP1, His Tag) Ala 2 - Lys 312 (Accession # AAH14051) was produced in E.coli cells at ACROBiosystems.

Molecular Characterization

Human AIMP1, His Tag is fused with a polyhistidine tag at the N-terminus, and has a calculated MW of 35.2 kDa. The predicted N-terminus is Met. The reducing (R) protein migrates as 36 kDa in SDS-PAGE .

Endotoxin

Less than 1.0 EU per μg by the LAL method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Trehalose are added as protectants before lyophilization.

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Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).

 

SDS-PAGE


Human AIMP1 / EMAP2 / SCYE1 Protein
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%.
 
 

Background

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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References

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