|HSPH1 in Rat Brain. HSPH1 was detected in perfusion fixed frozen sections of rat brain (cerebellum) using 5 µg/mL Human/Mouse/Rat HSPH1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4029) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.|
|Detection of Human/Mouse/Rat HSPH1 by Western Blot. Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line, DA3 mouse myeloma cell line, and NRK rat normal kidney cell line. PVDF membrane was probed with 0.1 µg/mL of Human/Mouse/Rat HSPH1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4029) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for HSPH1 at approximately 105-110 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
The heat shock proteins (HSPs) are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. Heat Shock Proteins are ubiquitously expressed in all organisms. They are induced in response to various types of environmental stresses like heat, cold, and oxygen deprivation. Heat shock protein H1 (HSPH1), also known as HSP105 and HSP110, exists as two isoforms, alpha and beta. HSPH1 alpha consists of 858 amino acids whereas HSPH1 beta has 814 amino acids. alpha and beta have calculated molecular weights of 96.4 kDa and 92 kDa, respectively, but an apparent molecular weight of 105‑110 kDa in SDS‑PAGE. HSPH1 acts as a chaperone to prevent thermal aggregation in mammalian cells. HSPH1 alpha and beta isoforms share 94% identity. Rat HSPH1 has 92% and 97% identity to human and mouse HSPH1, respectively.
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