Stress-Induced-phosphoprotein 1 (STIP1) ELISA Kits

Human Stress-Induced-phosphoprotein 1 (STIP1) interaction partners

1. Hop stabilises emerin and that loss of Hop alters nuclear structure via emerin degradation.

2. STIP1 acts as an oncogene in colorectal carcinoma and can therefore serve as a biomarker for the prognosis of patients with CRC.

3. Our findings indicate that elevated expression of STIP1 exhibited a metastasis-promoting effect in GC cells through activation of Wnt/beta-catenin signaling pathway.

4. STIP1 is positively associated with sublethal heat-induced cancer cell metastasis through mediating the mesenchymal gene transcription.

5. High STIP1 expression was significantly associated with shorter overall survival, earlier lymph node metastasis and more advanced clinical stage compared with low STIP1 expression in cancer. Therefore, STIP1 expression might be used as a prognostic biomarker for cancer treatment.

6. The G/G allele of stress induced phosphoprotein 1(STIP1) single nucleotide polymorphism rs4980524 is associated with the increased expression of STIP1 in endometriosis

7. Significant genetic association was identified at the rs2236647 (T/C) SNP in STIP1 and risk of asthma (p < 0.001). The C allele and CC genotype of this SNP were significantly higher in asthmatics compared with controls.

8. Functional studies showed that STIP1 promoted the growth, colony formation and migration of cancer cells. However, knocking down the expression of STIP1 inhibited the growth, colony formation and migration of cancer cells.

9. In vitro experiments revealed that STIP1 was capable of binding to the MMP-9 promoter and enhanced its transcriptional expression

10. STIP1 modulates the function of the HSP90-JAK2-STAT3 complex

11. Hsp70/Hsp90-organizing protein promoter activity was highest in Hs578T which expressed mutant or inactive p53. HRAS activation of the Hsp70/Hsp90-organizing protein promoter was inhibited by p53 overexpression.

12. the modulation of HOP-PrP(C) engagement or the decrease of PrP(C) and HOP expression may represent a potential therapeutic intervention in glioblastoma.

13. In conclusion, STIP1 is upregulated in HCC and associated with poor clinical prognosis. Blocking STIP1 activity suppresses HCC cell growth, providing the rationale for STIP1 as a potential therapeutic target in HCC.

14. Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 and STIP1 are key players in this pathway; the stoichiometry of S100A1/STIP1 interaction appears to be three S100A1 dimers plus one STIP1 monomer; each S100A1-STIP1-binding interaction is entropically driven. (S100A1 = S100 calcium binding protein A1; STIP1 = stress-induced-phosphoprotein 1) [REVIEW]

15. Results indicte the great potential of STIP1 (stress-induced phosphoprotein 1) as a biomarker and therapeutic target in renal cell carcinoma (RCC) bone metastasis.

16. Data suggest that three dimers of S100A1 (S100 calcium binding protein A1) associate with one molecule of STIP1 (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1.

17. Data confirmed the significant up-regulation of STIP1 in tumorous cholangiocytes relative to normal hepatocytes and non-tumorous cells and show prooved it as a reliable diagnostic biomarker when using immunohistochemistry.

18. STIP1 and moesin may be novel and differential sero-diagnostic markers for psoriasis vulgaris and psoriatic arthritis

19. Stip1 has a role in the male reproductive system and is expressed during the stress response

20. Increased STIP1 expression is associated with poor survival outcome in epithelial ovarian cancer (EOC), and STIP1 may represent a useful therapeutic target in EOC patients.

Mouse (Murine) Stress-Induced-phosphoprotein 1 (STIP1) interaction partners

1. Our experiments reveal that STI1 activates multiple signaling pathways that cooperate to increase neuronal resilience in neurons subjected to ischemic insult.

2. These results indicate that PrPC mutations impair cellular functions mediated by the wild-type protein in conjunction with STI1 in neural cells, supporting the hypothesis of a PrPC loss-of-function mechanism linked to prion disease.

3. In conclusion, STIP1 is upregulated in HCC and associated with poor clinical prognosis. Blocking STIP1 activity suppresses HCC cell growth, providing the rationale for STIP1 as a potential therapeutic target in HCC.

4. Domains of STIP1 responsible for regulating PrPC-dependent amyloid-beta oligomer toxicity

5. Reduced STIP1 levels can contribute to phenotypes related to hyperactivity and attention deficits.

6. We correlate the expression of STI1 and glioma progression, and suggest that STI1 expression in microglia/macrophages and infiltrating lymphocytes is modulated by the brain tumor microenvironment.

7. Knockdown of PIAS1 in astrocytes impairs the accumulation of nuclear STI1 in response to irradiation. Moreover, a PIAS1 mutant lacking the STI1 binding site is unable to increase STI1 nuclear retention.

8. stress-inducible protein-1 has a role in recruitment of bone marrow derived cells into the ischemic brains

9. Our findings reveal a previously unrecognized role of the PrP(C) ligand STI1 in protecting neurons in Alzheimer disease and suggest a novel pathway that may help to offset AbetaO-induced toxicity.

10. Stress-inducible phosphoprotein 1 has unique cochaperone activity during development and regulates cellular response to ischemia via the prion protein.

11. STI1 and laminin-gamma1 promote robust axonogenesis in wild-type dorsal root ganglia neurons; STI1 promotes extracellular calcium influx.

12. Neuroprotection and neuritogenesis mediated by PrP(C)-STI1 engagement are dependent upon the increased protein synthesis mediated by PI3K-mTOR signaling.

13. evaluated the temporal expression pattern of STI1 and Vn and their colocalization with their ligand PrPC, demonstrated that PrPC, STI1, and Vn are coexpressed in most of the embryonic tissues evaluated.

14. Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. The interaction sites were mapped to amino acids 113-128 from PrP(c) and 230-245 from STI1. Both proteins are associated in vivo.

15. mSTI1 has a specific tetratricopeptide repeat motif that enables it to bind to HSC70

16. first evidence of nuclear import and export of major Hsp70/Hsp90 co-chaperone mSTI1, and the regulation of this nuclear-cytoplasmic shuttling by cell cycle status and cell cycle kinases

17. These data are consistent with results established with a model where OR and N-terminal half of the HR mediate the action of STI1 upon cell survival and upregulation of SOD activity.

18. Stress-inducible protein 1 added to hippocampal cultures interacts with cellular prion protein (PrPc) and elicits neuritogenesis in wild-type neurons, but not PrPc-null cells.

19. This suggests an important role for Stip1 in the ability of germ cells to survive in stress conditions including high temperatures.

20. Hop may be cleaved by GzmB as an "innocent bystander" during the induction of apoptosis, but it may also act to facilitate apoptosis in concert with other GzmB substrates