| Product Name | STIP1, 1-543aa, Human |
|---|---|
| Description | STIP1, also known as stress-induced-phosphoprotein 1 isoform b, belongs to the large group of co-chaperones. The main function of STIP1 is to link Hsp70 and Hsp90 together. STIP1 also modulates the chaperone activities of the linked proteins and possibly interacts with other chaperones and proteins. It forms a complex with HSC70 and HSPCA/HSP-86 and HSPCB/HSP-84, as well as interacting with PACRG. Recombinant human STIP1 was expressed in E.coli and purified by using conventional chromatography techniques |
| Synonyms | Stress-induced-phosphoprotein 1 , STI1, HEl-S-94n, HOP, IEF-SSP-3521, P60, STI1L, Epididymis secretory sperm binding protein Li 94n HEL S 94n, Hop Hsc70/Hsp90 organizing protein, IEF SSP 3521 NY REN 11 antigen, P60 Renal carcinoma antigen NY-REN-11 STI1, STI1L, STIP1, STIP1_HUMAN Stress induced phosphoprotein 1 Transformation sensitive protein IEF SSP 3521 |
| Host | E. coli |
| Molecular Weight |
45.8kDa (407aa) 25-50kDa (SDS-PAGE under reducing conditions) |
| Amino Acid Sequence | MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLR NKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDK AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in Phosphate Buffered Saline (pH 7.4) containing 30% glycerol, 1mM DTT. |
| Concentration | 0.25mg/ml (determined by Absorbance at 280nm) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Johnson BD., et al. (1998) J Biol Chem. 273(6):3679-86. Van Der Spuy J., et al. (2001) Protein Expr Purif. 21(3):462-9. |
| Background | STIP1, also known as stress-induced-phosphoprotein 1 isoform b, belongs to the large group of co-chaperones. The main function of STIP1 is to link Hsp70 and Hsp90 together. STIP1 also modulates the chaperone activities of the linked proteins and possibly interacts with other chaperones and proteins. It forms a complex with HSC70 and HSPCA/HSP-86 and HSPCB/HSP-84, as well as interacting with PACRG. Recombinant human STIP1 was expressed in E.coli and purified by using conventional chromatography techniques |
| Supplier | ARP |
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