Recombinant Human HSP47 His-tag Protein, CF Summary
Ala19-Asp412, with a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and TCEP.|
|Reconstitution||Reconstitute at 500 μg/mL in water.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
2 μg/lane of Recombinant Human HSP47 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing a band at ~50 kDa under R conditions.
Heat Shock Protein 47 (HSP47), also known as Serpin-H1, is a 47 kDa collagen-binding stress protein localized in the endoplasmic reticulum (ER) of collagen-secreting cells (1). It is encoded by the SERPINH1 gene, belongs to the serpin family, and contains the typical serpin fold but has no serine protease inhibitory activity (1). Human HSP47 shares 96% aa sequence identity with mouse HSP47. HSP47 is a chaperone that specifically binds pro-collagens at a neutral pH via Gly-Xaa-Arg repeats located on triple-helical procollagen to prevent aggregate formation (2). HSP47 is required for correct procollagen folding in the ER (1). Expression of HSP47 is directly correlated with expression of collagens in multiple types of cells and tissues. Gene disruption of HSP47 in mice causes embryonic lethality due to defects in collagen biosynthesis (1, 3) and HSP47-knockout cells show abnormal helix formation resulting in thin, branched fibrils (1, 4). HSP47 is associated with collagen-related disorders such as osteogenesis imperfecta (5) and fibrosis of the liver, lung, and other organs (6, 7). Its role in collagen regulation, as well as its ability to cause ER stress-mediated apoptosis in collagen-producing cells (6), make HSP47 a promising target for treatment in collagen-related diseases (7, 8). Additionally, HSP47 modulates the tumor microenvironment (9) and may serve as a predictive marker in patients with colorectal, renal, and laryngeal squamous cell carcinomas (10-12).
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