Stress-Induced-phosphoprotein 1 Proteins (STIP1)

STIP1 is an adaptor protein that coordinates the functions of HSP70 (see HSPA1A\; MIM 140550) and HSP90 (see HSP90AA1\; MIM 140571) in protein folding.

list all proteins Gene Name GeneID UniProt
Mouse STIP1 STIP1 20867 Q60864
Rat STIP1 STIP1 192277 O35814
Human STIP1 STIP1 10963 P31948
How to order from antibodies-online
  • +1 877 302 8632
  • +1 888 205 9894 (toll-free)
  • Order online
  • orders@antibodies-online.com

Top Stress-Induced-phosphoprotein 1 Proteins at antibodies-online.com

Showing 3 out of 3 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Escherichia coli (E. coli) Human His tag 100 μg Log in to see 15 to 19 Days
$676.92
Details
Yeast Rat His tag   1 mg Log in to see 60 to 71 Days
$3,551.17
Details
Escherichia coli (E. coli) Human GST tag,His tag 100 μg Log in to see 15 to 18 Days
$714.00
Details

More Proteins for Stress-Induced-phosphoprotein 1 (STIP1) Interaction Partners

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

  1. In conclusion, STIP1 is upregulated in HCC (show FAM126A Proteins) and associated with poor clinical prognosis. Blocking STIP1 activity suppresses HCC (show FAM126A Proteins) cell growth, providing the rationale for STIP1 as a potential therapeutic target in HCC (show FAM126A Proteins).

  2. Domains of STIP1 responsible for regulating PrPC (show PRNP Proteins)-dependent amyloid-beta oligomer toxicity

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

  4. 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.

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

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

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

  8. Stress-inducible phosphoprotein 1 has unique cochaperone activity during development and regulates cellular response to ischemia via the prion protein (show PRNP Proteins).

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

  10. Neuroprotection and neuritogenesis mediated by PrP(C (show PRNP Proteins))-STI1 engagement are dependent upon the increased protein synthesis mediated by PI3K-mTOR (show FRAP1 Proteins) signaling.

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

  1. 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.

  2. In vitro experiments revealed that STIP1 was capable of binding to the MMP-9 (show MMP9 Proteins) promoter and enhanced its transcriptional expression

  3. STIP1 modulates the function of the HSP90 (show HSP90 Proteins)-JAK2 (show JAK2 Proteins)-STAT3 (show STAT3 Proteins) complex

  4. Hsp70/Hsp90-organizing protein promoter activity was highest in Hs578T which expressed mutant or inactive p53 (show TP53 Proteins). HRAS (show HRAS Proteins) activation of the Hsp70/Hsp90-organizing protein promoter was inhibited by p53 (show TP53 Proteins) overexpression.

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

  6. In conclusion, STIP1 is upregulated in HCC (show FAM126A Proteins) and associated with poor clinical prognosis. Blocking STIP1 activity suppresses HCC (show FAM126A Proteins) cell growth, providing the rationale for STIP1 as a potential therapeutic target in HCC (show FAM126A Proteins).

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

  8. Results indicte the great potential of STIP1 (stress-induced phosphoprotein 1) as a biomarker and therapeutic target in renal cell carcinoma (show MOK Proteins) (RCC (show XRCC1 Proteins)) bone metastasis.

  9. Data suggest that three dimers of S100A1 (S100 calcium binding protein A1 (show S100A1 Proteins)) 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 (show S100A1 Proteins) dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1 (show S100A1 Proteins).

  10. 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.

Stress-Induced-phosphoprotein 1 (STIP1) Protein Profile

Protein Summary

STIP1 is an adaptor protein that coordinates the functions of HSP70 (see HSPA1A\; MIM 140550) and HSP90 (see HSP90AA1\; MIM 140571) in protein folding. It is thought to assist in the transfer of proteins from HSP70 to HSP90 by binding both HSP90 and substrate-bound HSP70. STIP1 also stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones (Song and Masison, 2005

Gene names and symbols associated with STIP1

  • stress induced phosphoprotein 1 L homeolog (stip1.L)
  • stress induced phosphoprotein 1 (STIP1)
  • Stress-induced-phosphoprotein 1 (GL50803_27310)
  • stress-induced-phosphoprotein 1 (PGTG_06468)
  • stress induced phosphoprotein 1 (stip1)
  • stress induced phosphoprotein 1 S homeolog (stip1.S)
  • stress-induced phosphoprotein 1 (stip1)
  • stress-induced phosphoprotein 1 (Stip1)
  • stress induced phosphoprotein 1 (Stip1)
  • tuftelin interacting protein 11 L homeolog (tfip11.L)
  • HOP protein
  • IEF-SSP-3521 protein
  • MGC53256 protein
  • MGC76181 protein
  • MGC82554 protein
  • P60 protein
  • STI1 protein
  • STI1L protein
  • stip protein
  • stip1 protein
  • zgc:92133 protein

Protein level used designations for STIP1

stress-induced-phosphoprotein 1 , stress-induced-phosphoprotein 1 (Hsp70/Hsp90-organizing protein) , Stress-induced-phosphoprotein 1 , Hsp70/Hsp90 organizing protein , IEF SSP 3521 , hsc70/Hsp90-organizing protein , mSTI1 , stress-inducible protein , STI1 , hop , Hsc70/Hsp90-organizing protein , Hsp70/Hsp90-organizing protein , NY-REN-11 antigen , renal carcinoma antigen NY-REN-11 , transformation-sensitive protein IEF SSP 3521 , STIP-1 , septin and tuftelin-interacting protein 1 , tuftelin-interacting protein 11

GENE ID SPECIES
379955 Xenopus laevis
451286 Pan troglodytes
717926 Macaca mulatta
5697231 Giardia lamblia ATCC 50803
10539523 Puccinia graminis f. sp. tritici CRL 75-36-700-3
100356266 Oryctolagus cuniculus
394990 Xenopus (Silurana) tropicalis
447010 Xenopus laevis
493606 Danio rerio
20867 Mus musculus
192277 Rattus norvegicus
100689413 Cricetulus griseus
10963 Homo sapiens
474837 Canis lupus familiaris
617109 Bos taurus
447466 Xenopus laevis
Did you look for something else?