HSP70
HSP70 is the chaperone partner recognised by the ST13 gene product, the Hsc70-interacting protein (HIP, also known as SNC6, HSPABP1, P48 and FAM10A1). This cytoplasmic adaptor protein mediates the association of the heat shock proteins HSP70 and HSP90 and stabilises a substrate-binding state of HSC70. Browse Assay Genie's current range of HSP70 research reagents below, or read on for the biology behind the target.
The protein encoded by ST13 is an adaptor that mediates the association of the heat shock proteins HSP70 and HSP90. Its mechanism has been described in detail for HSC70: one HIP oligomer binds the ATPase domains of at least two HSC70 molecules, in a manner that depends on activation of the HSC70 ATPase by HSP40. In doing so it stabilises the ADP state of HSC70, which has a high affinity for substrate protein. Through its own chaperone activity, it may also contribute to the interaction of HSC70 with various target proteins.
The ST13 gene (ST13 Hsp70 interacting protein) encodes a cytoplasmic protein that belongs to the FAM10 family and sits within the HGNC gene group of tetratricopeptide repeat domain containing proteins. Alternative splicing results in multiple transcript variants encoding different isoforms. Orthologous genes, named St13, are present in both mouse and rat, which allows the HSP70-interacting protein to be studied in common rodent models.
Functionally, the protein has been shown to be involved in the assembly of the glucocorticoid receptor, a process that requires the assistance of multiple molecular chaperones. Expression of the gene is reported to be downregulated in colorectal carcinoma tissue, which suggests it may act as a candidate tumour suppressor gene. This is reflected in its earlier name, suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein). Other aliases and previous symbols include SNC6, HSPABP1, HIP, P48 and FAM10A1, so literature searches for this target should take account of all of them.
HIP stabilises the high-substrate-affinity ADP state of HSC70, making it a useful subject for studying how co-chaperones regulate HSP70-family activity.
As an adaptor linking HSP70 and HSP90, the protein is relevant to studies of how multichaperone complexes are built.
The protein is involved in glucocorticoid receptor assembly, which depends on the combined action of several molecular chaperones.
Reduced expression in colorectal carcinoma tissue has led to ST13 being considered a candidate tumour suppressor gene.
It is an adaptor protein that mediates the association of HSP70 and HSP90. One HIP oligomer binds the ATPase domains of at least two HSC70 molecules and stabilises the ADP state, which has a high affinity for substrate protein. It may also contribute through its own chaperone activity.
ST13 is also called Hsc70-interacting protein, HIP, SNC6, HSPABP1, P48 and FAM10A1. Its earlier name was suppression of tumorigenicity 13 (colon carcinoma). Alternative splicing produces multiple transcript variants that encode different isoforms.
Mouse and rat both carry an orthologous St13 gene; check the datasheet of any product for its validated reactivity. ST13 expression is reported to be downregulated in colorectal carcinoma tissue, so it is regarded as a candidate tumour suppressor gene.
Other targets with neighbouring gene symbols that have pages at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P50502; product specifications from Assay Genie datasheets.