Recombinant Human STIP1/STI1 protein (DDDDK tag N-Terminus)
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Recombinant Human STIP1/STI1 protein (DDDDK tag N-Terminus) is a Human Full Length protein, in the 2 to 543 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
Stress-induced-phosphoprotein 1, STI1, Hsc70/Hsp90-organizing protein, Renal carcinoma antigen NY-REN-11, Transformation-sensitive protein IEF SSP 3521, Hop, STIP1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human STIP1/STI1 protein (DDDDK tag N-Terminus) (AB196404)
4-20% SDS-PAGE analysis of 2 μg ab196404 with Coomassie staining.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The stress-induced phosphoprotein STIP1 functions within cytoplasm and is pivotal for cellular integrity. It forms a complex with HSP70 and HSP90 that regulates the folding and activation of a range of client proteins including steroid hormone receptors and kinases. This modulation influences protein activity stability and degradation. STIP1 impacts signal transduction pathways cellular growth and stress responses by influencing how effectively client proteins perform their biological roles within cells.
Pathways
The protein STIP1 plays a significant part in the steroid hormone signaling pathway and the protein folding network. It helps facilitate the proper folding and function of steroid hormone receptors through its interaction with major chaperone proteins HSP70 and HSP90. Both these pathways are important for cell survival and proper cell regulation. By helping with the maturation and activation of client proteins STIP1 ensures that cellular responses to various internal and external signals proceed efficiently.
Specifications
Form
Liquid
General info
Function
Acts as a co-chaperone for HSP90AA1 (PubMed : 27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity).
Subcellular localisation
Nucleus
Target data
Product promise
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