Transfected Stable Cell Lines
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Precision reporter, kinase, immune receptor, biosimilar, Cas9, and knockout stable cell lines for diverse applications.
| Cat.No. | Product Name | Price |
|---|---|---|
| CSC-DC004723 | Panoply™ Human EEF1A1 Knockdown Stable Cell Line | Inquiry |
| CSC-SC004723 | Panoply™ Human EEF1A1 Over-expressing Stable Cell Line | Inquiry |
| CSC-RO01366 | Mouse Eef1a1 Stable Cell Line - RAW 264.7 | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| AD05271Z | Human EEF1A1 adenoviral particles | Inquiry |
| LV11441L | human EEF1A1 (NM_001402) lentivirus particles | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| SHW004676 | shRNA set against Chicken EEF1A1 (NM_204157) | Inquiry |
| SHG153979 | shRNA set against Human EEF1A1(NM_001402.5) | Inquiry |
| SHH024527 | shRNA set against Mouse Eef1a1(NM_010106.2) | Inquiry |
| SHH024545 | shRNA set against Rat Eef1a1(NM_175838.1) | Inquiry |
| SHH283261 | shRNA set against Mouse EEF1A1 (NM_010106.2) | Inquiry |
| SHH283265 | shRNA set against Rat EEF1A1 (NM_175838.1) | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| CDCB159411 | Human EEF1A1 ORF clone (BC008587) | Inquiry |
| CDCB180421 | Rabbit EEF1A1 ORF clone (NM_001082339.1) | Inquiry |
| CDCR248436 | Mouse Eef1a1 ORF Clone(NM_010106.2) | Inquiry |
| CDFR014876 | Rat Eef1a1 cDNA Clone(NM_175838.1) | Inquiry |
| MiUTR1H-03113 | EEF1A1 miRNA 3'UTR clone | Inquiry |
| MiUTR1M-04177 | EEF1A1 miRNA 3'UTR clone | Inquiry |
| MiUTR1R-01650 | EEF1A1 miRNA 3'UTR clone | Inquiry |
| CDCB156105 | Cynomolgus EEF1A1 ORF clone | Inquiry |
| CDCB157084 | Mouse EEF1A1 ORF clone (AK137223.1) | Inquiry |
| CDCB166151 | Chicken EEF1A1 ORF Clone (NM_204157) | Inquiry |
| CDCR280692 | Human EEF1A1 ORF Clone(NM_001402.5) | Inquiry |
| CDCR381923 | Rat Eef1a1 ORF Clone(NM_175838.1) | Inquiry |
| CDCS410260 | Human EEF1A1 ORF Clone (BC008587) | Inquiry |
Eukaryotic translation elongation factor 1A1 (eEF1A1) is an important factor that plays a role in peptide chain elongation during protein synthesis and plays an important role in cell growth. The role of eEF1A1 is not limited to the extension of the peptide chain but also participates in physiological activities such as post-translational modification of proteins, protein degradation, and regulation of the cytoskeleton. These non-canonical functions play an important role in cell proliferation, apoptosis, and tumor cell invasion and metastasis. Interfering with the expression of eEF1A1 may affect the sensitivity of tumor chemotherapy, and eEF1A1 may become a potential target for tumor control.
The eEF1A1 protein is widely expressed in human tissues and is only found in adult striated muscle and myocardium. The content of eEF1A1 protein in eukaryotic cells is second only to actin, accounting for 1% to 3% of total protein in cells. eEF1A1 acts as a GTP-linked protein with three distinct domains, of which domain I binds to GTP, domain II binds to tRNA, and domains II and III are also involved in actin binding.
In the cytoplasm, eEF1A1 may be involved in the cytoplasmic retention of the amplified poly(A) protein, and aggregation of poly(A) may play a toxic role. When knocking out eEF1A1 expression, the amplified poly(A) protein remains in the nucleus to regulate gene transcription. In the cytoplasm, the cytoplasmically amplified poly(A) protein induces reduced toxicity. Li et al.'s study linked the expanded poly(A) protein nuclear output to its neurotoxicity and identified eEF1A1 as a regulator of diffuse poly(A) nuclear export and poly(A) disease toxicity.
Figure 1. Working model of eEF1A1 regulation of localization of expanded poly(A) tract-containing proteins in the cytoplasm. (Li, et al. 2017)
Correlation Between eEF1A1 and Tumor
eEF1A1 is highly expressed in malignant tumors such as leukemia, liver cancer, prostate cancer and breast cancer, and its abnormal expression is closely related to tumor formation, migration, and prognosis of patients. Chen et al. found that eEF1A1 expression was elevated in hepatocellular carcinoma (HCC) cell lines and clinical samples at the mRNA and protein levels. Immunohistochemistry showed that eEF1A1 expression was up-regulated in HCC samples compared to the corresponding non-tumor tissues. eEF1A1 acts as a substrate for FAT10 (HLA-F adjacent transcript 10) and plays a role in the development and progression of hepatocellular carcinoma.
Huang et al. found that eEF1A1 regulates the expression of cyclin D1 through STAT1 signaling in HCC to regulate the G1 phase of the cell cycle to promote tumor proliferation. In the study of prostate cancer, eEF 1A1 may be a downstream target gene that promotes prostate cancer proliferation by the homeobox gene Gbx 2 (gastrulation brain homeobox 2). In the study of prostate cancer bone metastasis, it was found that eEF1A1 was highly expressed in adjacent cancerous osteoblasts, which indicates that eEF1A1 may become a serum marker of prostate cancer. The researchers found that high expression of eEF1A1 was positively correlated with cell metastatic potential in rat breast cancer cells, and eEF1A1 expression was significantly higher in metastatic cells than in non-metastatic cells. In metastatic cells, eEF1A1 can exert a potentiating ability to enhance metastasis by attenuating binding to actin.
eEF1A1 and Tumor Cell Invasion and Metastasis
eEF1A1 is a multifunctional protein that also plays an important role in the regulation of the cytoskeleton and tubulin networks, which can directly or indirectly affect the ability of cells to invade and migrate. The study found that eEF1A1 in hepatocellular carcinoma can bind to the 5'-untranslated region (5'-UTR) of osteopontin mRNA, regulate the half-life of osteopontin mRNA, and reduce the expression level of osteopontin. This can affect the invasive ability of hepatocellular carcinoma. eEF1A1 also binds to the SAM (sterile alpha motif) domain of deleted in liver cancer 1 (DLC1), which promotes the aggregation of eEF1A1 at the cell membrane site and inhibits cell migration. The binding of SAM-eEF1A1 is important in GTPase-activating protein (GAP)-dependent cell migration. When the DLC1 and eEF1A1 binding sites are mutated, the role of DLC1 in inhibiting cell migration disappears, leading to an increase in the invasive ability of tumor cells.
The study found that heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) can inhibit a variety of gene translation processes that play an important role in EMT, and this effect is achieved by the formation of a complex between eEF1A1 and hnRNP E1. When eEF1A1 binds to hnRNP E1, eEF1A1 at the ribosomal A site, the conformation of eEF1A1 binding to GDP no longer changes, leaving eEF1A1 · GDP to stay on the ribosome, causing translational silencing of EMT-related genes.
The sensitivity of eEF1A1 and Tumor Chemotherapy
Chemotherapy is one of the important methods of cancer treatment. However, in some malignant tumors, insensitivity or ineffectiveness often occurs, which is a major problem that plagues tumor treatment. Recent studies have shown that down-regulation of eEF1A1 expression may sensitize tumor chemotherapy, making it a potential tumor therapeutic target. Blanch et al. found that eEF1A1 binds to p53 family proteins, and the abnormally increased eEF1A1 protein in tumor cells inhibits the p53 family-mediated pro-apoptotic effect, thereby counteracting the killing effect of chemotherapeutic drugs on tumor cells. Interfering with eEF 1A1 promoted apoptosis of p53 wild-type tumor cells, suggesting that eEF1A1 is an inhibitor of apoptosis induced by p53 family proteins. After the chemotherapy drug combination interference eEF 1A1, apoptosis of tumor cells rose significantly, and its mechanism may be related to the p53 family.
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