Recombinant Human Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 1 Protein (AIMP1), Active

Name: Recombinant Human Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 1 Protein (AIMP1), Active
Brand: Beta LifeScience
SKU: BLC-05664P
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 1 Protein (AIMP1), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 98% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The ED50 as determined by the apoptotic effect using serum free human MCF-7 cells is less than 40 ng/ml, corresponding to a specific activity of >2.5x10 4 IU/mg.
Uniprotkb	Q12904
Target Symbol	AIMP1
Synonyms	AIMP 1; Aimp1; AIMP1/p43; AIMP1_HUMAN; Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1; ARS interacting multifunctional protein 1; EMAP 2; EMAP-2; EMAP-II; EMAP2; EMAPII; Endothelial monocyte activating polypeptide 2; Endothelial monocyte activating polypeptide; Endothelial monocyte-activating polypeptide 2; Endothelial monocyte-activating polypeptide II; HLD3; Multisynthase complex auxiliary component p43; Multisynthetase complex auxiliary component p43; OTTHUMP00000219673; p43; Scye 1; Scye1; Scye1, formerly; Small inducible cytokine subfamily E member 1; Small inducible cytokine subfamily E, member 1 (endothelial monocyte-activating); Small inducible cytokine subfamily E, member 1, formerly
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK
Expression Range	147-312aa
Protein Length	Partial
Mol. Weight	18.2 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered PBS, pH 7.4
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.
Subcellular Location	Nucleus. Cytoplasm, cytosol. Secreted. Endoplasmic reticulum. Golgi apparatus.
Database References	HGNC: 10648 OMIM: 260600 KEGG: hsa:9255 STRING: 9606.ENSP00000378191 UniGene: PMID: 29537208 This study showed the potential of the anti-AIMP1 antibody as a therapeutic option for AD treatment. Also, the finding of an association of blood AIMP1 levels with the MMSE score. PMID: 27906773 systemic mRNA expression of AIMP1 strongly differentiated children who failed to achieve asthma control with triamcinolone administration PMID: 27665382 p43 induces both the mRNA and protein expression of IP-10. PMID: 27574027 Data indicate that AIMP1 downregulation using siRNA is a novel tool to restore TGF-beta signaling and thereby increases the chondrogenic potential of dedifferentiated/degenerated chondrocytes. PMID: 26890138 two homozygous missense variants, p.(Gly299Arg) and p.(Val176Gly), in the gene AIMP1 that co-segregated with the phenotype, are reported. PMID: 26173967 findings suggest EMAP II is elevated in type 1 diabetic patients, particularly those with micro-vascular complications; EMAP II levels are related to inflammation, glycemic control, albuminuria level of patients and the risk of micro-vascular complications PMID: 26142824 AIMp1 promotes the proliferation and migration of fibroblasts/endothelial cells and importantly, pro-inflammatory gene expression in monocytes/macrophages and dendritic cells. PMID: 26325028 Increased serum level of EMAP-II may be one of the pathways of endothelial dysfunction in type 1 diabetes. PMID: 27089716 AIMP1 appears to function as a novel inhibitor of PPARgamma that regulates adipocyte differentiation by preventing the transcriptional activation of PPARgamma. PMID: 25146391 Data indicate that HCV E2 glycoprotein interacts with cellular AIMP1/p43 protein and promotes cell surface expression of membrane glycoproteins gp96 and transforming growth factor beta TGF-beta signaling. PMID: 24816397 Data indicate that the N terminus of Pro-EMAP II binds to its C terminus, arginyl-tRNA synthetase, and the neurofilament light subunit. PMID: 25724651 EMAP2 is a multifunctional polypeptide with proinflammatory and antiangiogenic activity. (Review) PMID: 26040042 Kisspeptin effect on endothelial monocyte activating polypeptide II (EMAP-II)-associated lymphocyte cell death and metastases in colorectal cancer patients PMID: 24395571 interactions between the N-terminal domains of ArgRS and AIMP1 are important for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex with ArgRS-GlnRS-AIMP1 PMID: 25288775 vascular contribution to lung development and the implications that vascular mediators such as EMAP II have in distal lung formation during the vulnerable stage of alveolar genesis. PMID: 24619875 AIMP1 peptide promotes the proliferation of BMMSCs by activating the beta-catenin/TCF complex via FGFR2-mediated activation of Akt, which leads to an increase in mesenchymal stem cells in peripheral blood. PMID: 23672191 Downregulation of CD23 attenuated AIMP1-induced TNF-alpha secretion and AIMP1 binding. PMID: 22767513 EMAP-II transcripts are upregulated in tumour cells in hypoxic conditions. PMID: 23082492 EMAP II has specific intracellular effects, and that this intracellular function appears to antagonize its extracellular anti-angiogenic effects during fetal development and pulmonary disease progression. PMID: 22412987 we propose that AIMP1 effect on EC adhesion is mediated by the assembly of a cytoskeletal protein complex on the cytosolic face of the cell membrane PMID: 21416500 Decreased expression of AIMP1 in gastric and colorectal cancer tissues suggests that down-regulation of this protein may be related to inactivation of the tumor suppressor functions of AIMP proteins and might play a role in the development of GC and CRC. PMID: 21789020 EMAPII is elevated in the BALF of active smokers and patients with COPD. Expression was increased in COPD lungs and emphysema. PMID: 21576822 The known pathological functions together with abundant cellular accumulation in cerebral ischemia lesions suggest that EMAPII might contribute to pathophysiological consequences of cerebral ischemia. PMID: 21047177 Through genome-wide homozygosity mapping and mutation analysis, we demonstrated in all affected individuals a homozygous frameshift mutation that fully abrogates the main active domain of AIMP1 PMID: 21092922 autoantibodies of aminoacyl-tRNA synthetase can be used in the diagnosis of type I diabetes PMID: 20429837 LPS induces the dissociation of gp96 from AIMP1 by phosphorylation through TLR4/MyD88-mediated JNK activation, resulting in translocation of gp96 on the cell surface. PMID: 20510162 p43 is cleaved during apoptosis by calpains and released as a truncated protein that is harmless for the structure of the atherosclerotic plaque. PMID: 20413730 AIMP1 may exert its antitumor activity by inducing tumor-suppressing cytokines. After a single intravenous injection, AMP1 exhibited a low clearance showing a one-compartmental disposition. PMID: 19573982 These results suggest the potential interaction of p43/EMAP II with alpha-ATP synthase and its role in the proliferation of endothelial cells. PMID: 11741979 temporal variation in EMAP II expression in the human endometrium across the menstrual cycle and localize expression to glandular epithelial, endothelial, and stromal cells. Moreover, EMAP II expression is negatively regulated by PGE(2). PMID: 12161535 p43-induced TNF production was mediated by the activation of MAPK family members, ERK and p38 MAPK, and by IkappaB degradation leading to the activation of NFkappaB. PMID: 12543078 Expression of endothelial monocyte activating polypeptide II is increased after spinal cord injury (SCI), suggesting a role for EMAP II in the pathophysiology of secondary injury following SCI. PMID: 14588117 Membrane-bound and soluble EMAP-II appear to play multiple roles in the tumor microenvironment, one of which is to assist in immune evasion. PMID: 14688335 EMAP-II causes a dose-dependent inhibition of proliferation and apoptosis in Jurkat T cells and mitogen-activated peripheral blood mononuclear cells, suggesting that EMAP-II constitutes a component of a novel, immunosuppressive pathway in solid tumors PMID: 14982944 DOC1 might play a role in mediating some of the effects of EMAP-II on endothelial cells PMID: 15935955 EMAP II is cleaved by MMP-9, elastase, and cathepsin L. PMID: 16674941 Three-dimensional structure is projected from amino acid sequence. PMID: 17018011 suggest that the cleavage of p43 and its cellular delocalization PMID: 17303557 Arginyl t-RNA synthetase over-expression associates with a reduced AIMP1 secretion. Multicatalytic protease is involved in the generation of the mature cytokine, EMAP II. PMID: 17443684 serum EMAP-II levels are significantly higher in patients with NSCLC than in healthy subjects and suggest it is of potential prognostic value PMID: 18621627 Results suggest novel roles for EMAP II in modulating the migration of dendritic cells and suggest that these effects may modify Meth A tumor/host interactions. PMID: 18951814 Inhibition of VEGF signaling is one possible antiangiogenic mechanism of EMAP II, which may explain its in vivo antitumor activity and delineate therapeutic strategies to enhance anti-VEGF therapy to inhibit tumor growth. PMID: 19002109 one of the major anti-angiogenic functions of EMAP-II is exerted through its inhibition of the HIF-1alpha activities PMID: 19362550 EMAP-II plays an important role in endothelial cell dysfunction related to graft-versus-host disease after allogeneic stem cell transplantation. PMID: 19565673 this is the first report showing evidence for the chemoattractant properties of EMAPII on leech and human microglial cells PMID: 19917687 Expression of the cleaved EMAP-II form in tumour-biopsies correlates with a good response of melanoma patients to TNF-based ILP. PMID: 16615114 EMAP-II facilitates apoptotic signaling of TNF-R1 via mobilization of TRADD. PMID: 17051333

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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