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|Recombinant Human AIMP1 / EMAP II / SCYE1 protein (Catalog#10623-H07E)|
|0.2 μm filtered solution in PBS with 5% trehalose|
|Produced in rabbits immunized with purified, recombinant Human AIMP1 / EMAP II / SCYE1 (rh AIMP1 / EMAP II / SCYE1; Catalog#10623-H07E; NP_004748.2; Ala 2-Lys 312). AIMP1 / EMAP II / SCYE1 specific IgG was purified by Human AIMP1 / EMAP II / SCYE1 affinity chromatography.|
|Human AIMP1 / EMAP II / SCYE1|
ELISA: 0.1-0.2 μg/mL
This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect Human SCYE1.
IHC-P: 0.1-2 μg/mL
|This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.|
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Immunochemical staining of human SCYE1 in human brain with rabbit polyclonal antibody (1 µg/mL, formalin-fixed paraffin embedded sections).
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, also known as Multisynthase complex auxiliary component p43, Endothelial monocyte-activating polypeptide II, AIMP1, EMAP2 and SCYE1, is a nucleus protein which contains one tRNA-binding domain. AIMP1 (also known as p43) is a factor associated with a macromolecular aminoacyl-tRNA synthetase (ARS) complex but also plays diverse regulatory roles in various physiological processes. AIMP1 negatively regulates TGF-beta signaling via stabilization of Smurf2. It suggests the novel activity of AIMP1 as a component of negative feedback loop of TGF-beta signaling. Recently, it been demonstrated that AIMP1 is also secreted and acts as a novel pleiotropic cytokine. AIMP1 protein induces the maturation and activation of DCs, which skew the immune response toward a Th1 response. AIMP1 is known as a cytokine working in the control of angiogenesis, inflammation, and wound healing. AIMP1 is secreted from the pancreas upon glucose starvation, and it also plays a glucagon-like role in glucose homeostasis. Although AIMP1 was identified as a component of the macromolecular aminoacyl tRNA synthetase complex involved in the cellular translation process, it was also found to be secreted as a cytokine having complex physiological functions. Among these, AIMP1's angiostatic and immune stimulating activities suggest its potential use as a novel antitumor therapeutic protein. AIMP1 may exert its antitumor activity by inducing tumor-suppressing cytokines. Thus, AIMP1 may be useful as a novel anti-tumor agent.