| Alternative Name: | HSC70-interacting protein |
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| MW: | ~54kDa |
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| Source: | Produced in E. coli. |
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| UniProt ID: | P50503 |
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| Formulation: | Liquid. In 20mM MOPS, pH 7.2, containing 50mM sodium chloride and 2mM magnesium chloride. |
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| Purity: | ≥85% (SDS-PAGE; Western blot) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Applications: | WB
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| Application Notes: | Western blot control. |
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| Shipping: | Shipped on Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | Hsc70-interacting protein (Hip) is a cytosolic protein that exists as a homo-oligomer and participates in the regulation of the heat shock protein Hsc70 in eukaryotic cells. Hip interacts with the ATPase domain of Hsc70 molecules through the tetratricopeptide repeats and flanking charged α-helices of Hip. This binding reaction is dependent on Hsp40 in the presence of ATP and becomes Hsp40-independent if Hsc70 is preincubated with ADP. Upon binding to Hsc70, Hip stabilizes the ADP-bound state of Hsc70, a conformation that has a high affinity for unfolded substrate proteins. Hip by itself binds unfolded polypeptides, suggesting that it may possess chaperone activity. Together with Hsp40, Hip may regulate the chaperone activity of Hsc70 by stabilizing the chaperone-substrate complex |
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| Regulatory Status: | RUO - Research Use Only |
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