STIP1 Antibody

1. The G/G allele of stress induced phosphoprotein 1(STIP1) single nucleotide polymorphism rs4980524 is associated with the increased expression of STIP1 in endometriosis PMID: 29673672
2. 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. PMID: 29749828
3. 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. PMID: 29596884
4. In vitro experiments revealed that STIP1 was capable of binding to the MMP-9 promoter and enhanced its transcriptional expression PMID: 29304094
5. STIP1 modulates the function of the HSP90-JAK2-STAT3 complex PMID: 27409672
6. 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. PMID: 27987076
7. the modulation of HOP-PrP(C) engagement or the decrease of PrP(C) and HOP expression may represent a potential therapeutic intervention in glioblastoma. PMID: 28412969
8. 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. PMID: 28887036
9. 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] PMID: 28819010
10. Results indicte the great potential of STIP1 (stress-induced phosphoprotein 1) as a biomarker and therapeutic target in renal cell carcinoma (RCC) bone metastasis. PMID: 28199984
11. 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. PMID: 28408431
12. 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. PMID: 25034945
13. STIP1 and moesin may be novel and differential sero-diagnostic markers for psoriasis vulgaris and psoriatic arthritis PMID: 25010044
14. Stip1 has a role in the male reproductive system and is expressed during the stress response PMID: 25311551
15. 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. PMID: 24488757
16. our findings provide evidences that positive expression of STIP1 in papillary thyroid carcinoma may be important in the acquisition of an aggressive phenotype PMID: 24163084
17. These results indicate that HOP is a unique co-chaperone that undergoes an ATP-dependent conformational change. PMID: 24535459
18. STIP1 histoscores may be useful in detecting invasive human ovarian cancer in patients with low serum CA125 levels. PMID: 23915849
19. stress-inducible protein-1 has a role in recruitment of bone marrow derived cells into the ischemic brains PMID: 23836498
20. results show phosphorylation of the C-terminal region of Hsp70 and Hsp90 is critical for the decision between folding or degradation of client proteins by altering the binding of CHIP and HOP; also show increased phosphorylation in cancer cells with increased levels of the co-chaperone HOP PMID: 22824801
21. Luminal iron levels govern intestinal tumorigenesis after Apc loss in vivo. PMID: 22884369
22. HOP as a novel regulator of angiogenesis that functions through promoting vascular endothelial cell polarization and migration PMID: 22558459
23. STIP-1 is an antigenic target in cultured hippocampal neurons in sera and/or cerebrospinal fluids of patients with neuro-Behcet's disease. PMID: 21875754
24. We found no genome-wide statistically significant associations but identified several plausible candidate genes among findings at p < 5E-05: STIP1, TMEM132D, LRRC7, SEMA3A, and ALK. PMID: 21784300
25. High STIP1 is associated with pancreatic Cancer. PMID: 21470770
26. This study has revealed that Rho GDP-dissociation inhibitor 2, Y-box binding protein 1, and the HSP70/90 organizing protein have a critical role to play in resistance to cyclin-depedent kinases inhibitor. PMID: 21067243
27. show that stress-induced phosphoprotein 1 (STIP1) was secreted by ovarian cancer tissues into the peripheral blood of patients, resulting in a significant increase of serum levels of STIP1 in cancer patients compared with those in normal controls PMID: 20501939
28. Presented: Hop-D456G, a Hop mutant within the TPR2B-domain, that is a mixture of monomeric and dimeric species, suggesting the TPR2B-domain may also play a role in dimerization. PMID: 19961430
29. Sedimentation equilibrium AUC clearly shows that HOP is a monomer, with no indication of higher MW species. An in vivo coexpression assay that also supports the conclusion that HOP is a monomer. PMID: 19866486
30. TPR1 and TPR2A domains of the Hsp70/Hsp90 adapter protein p60/Hop specifically bind to short peptides corresponding to the C-terminal tails of Hsp70 and Hsp90 PMID: 11877417
31. Hsp70/Hsp90 organizing protein (Hop) coordinates Hsp70 and Hsp90 interactions during assembly of steroid receptor complexes. PMID: 15632128
32. STI1 is secreted by and induces proliferation in glioma cells, an effect that is modulated by the Erk and PI3K pathways. STI1 does not induce proliferation of normal glia, in contrast to glioma cells. PMID: 17886292
33. It is likely that Hop binds to both monomers of Hsp90 in the form of a clamp, interacting with residues in the middle domain of Hsp90, preventing ATP hydrolysis, possibly by the preventing binding of N-terminal and middle domains in Hsp90 monomers. PMID: 18485364
34. STIP1 genetic variations might play a role in regulating corticosteroid response in asthmatic subjects with reduced lung function. PMID: 19254810

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HGNC: 11387

OMIM: 605063

KEGG: hsa:10963

STRING: 9606.ENSP00000305958

UniGene: Hs.337295