IGF-II mRNA-binding proteins (IMPs) bind RNA and influence RNA synthesis and metabolism. IMP-1, also known as coding region determinant-binding protein/insulin-like growth factor II mRNA-binding protein (CRD-BP) and VICKZ1; IMP-2 (IMP2, VICKZ2, p62); and IMP-3 (KOC1, VICKZ3) contain a unique combination of RNA recognition motifs and four hnRNP K homology domains. IMP-1 is abundant in embryonal tissues and is expressed in 81% of colon cancers, 73% of sarcomas and 58.5% of breast cancers. It recognizes c-Myc, IGF-II and t mRNAs, and H19 RNA, and plays a major role in proliferation of K-562 cells by an IGF-II-dependent mechanism. IMP-2 binds the 5' UTR of IGF-II mRNA and influences tumor cell growth, in which IMP-2 is associated with apoptosis induced by tretinoin. IMP-3 knockdown by RNA interference decreases levels of IGF-II protein without affecting IGF-II, c-Myc, or β Actin mRNA and H19 RNA levels. IMP-3 is a marker for carcinomas and high-grade dysplastic lesions of pancreatic ductal epithelium.
Background References
1. Davidson, B. et al. VICKZ2 protein expression in ovarian serous carcinoma effusions is associated with poor survival. Human pathology. 45: 1520-8 (2014).
2. Rivera Vargas, T. et al. Post-transcriptional regulation of cyclins D1, D3 and G1 and proliferation of human cancer cells depend on IMP-3 nuclear localization. Oncogene (2013).
Sequence Similarity
Belongs to the RRM IMP/VICKZ family.
Tissue Specificity
Expressed in fetal liver, fetal lung, fetal kidney, fetal thymus, fetal placenta, fetal follicles of ovary and gonocytes of testis, growing oocytes, spermatogonia and semen (at protein level). Expressed in cervix adenocarcinoma, in testicular, pancreatic and renal-cell carcinomas (at protein level). Expressed ubiquitously during fetal development at 8 and 14 weeks of gestation. Expressed in ovary, testis, brain, placenta, pancreatic cancer tissues and pancreatic cancer cell lines.
Western blot analysis of IMP3 on different lysates with Rabbit anti-IMP3 antibody (R1512-10) at 1/1,000 dilution.
Lane 1: HeLa cell lysate Lane 2: 293T cell lysate Lane 3: MCF7 cell lysate Lane 4: THP-1 cell lysate
Lysates/proteins at 10 µg/Lane.
Predicted band size: 64 kDa Observed band size: 70 kDa
Exposure time: 2 minutes;
4-20% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (R1512-10) at 1/1,000 dilution was used in 5% NFDM/TBST at 4℃ overnight. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1/50,000 dilution was used for 1 hour at room temperature.
☑ Knockdown (KD)
Western blot analysis of IMP3 on different lysates with Rabbit anti-IMP3 antibody (R1512-10) at 1/2,000 dilution.
Lane 1: HAP1-parental cell lysate Lane 2: HAP1-IMP3 KD cell lysate
Lysates/proteins at 10 µg/Lane.
Predicted band size: 64 kDa Observed band size: 64 kDa
Exposure time: 3 seconds; ECL: K1801;
4-20% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (R1512-10) at 1/2,000 dilution was used in primary antibody dilution (K1803) at 4℃ overnight. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1/50,000 dilution was used for 1 hour at room temperature.
Immunohistochemical analysis of paraffin-embedded rat brain tissue using anti-IMP-3 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded human placental tissue using anti-IMP-3 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded mouse testis tissue using anti-IMP-3 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded mouse brain tissue with Rabbit anti-IMP3 antibody (R1512-10) at 1/400 dilution.
The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 1% BSA for 20 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (R1512-10) at 1/400 dilution for 1 hour at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
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