Detection of Human, Mouse, and Rat HSP70/HSPA1A by Western Blot. |
Western blot shows lysates of Jurkat human acute T cell leukemia cell line, HeLa human cervical epithelial carcinoma cell line, L‑929 mouse fibroblast cell line, and C6 rat glioma cell line. PVDF membrane was probed with 0.1 µg/mL of Rabbit Anti-Human/Mouse/Rat HSP70/HSPA1A Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1663) followed by HRP-conjugated Anti‑Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for HSP70/HSPA1A at approximately 72 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.
|Detection of Human and Mouse HSP70/HSPA1A by Simple WesternTM. Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line and C2C12 mouse myoblast cell line, loaded at 0.2 mg/mL. A specific band was detected for HSP70/HSPA1A at approximately 66 kDa (as indicated) using 0.5 µg/mL of Rabbit Anti-Human/Mouse/Rat HSP70/HSPA1A Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1663). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.|
Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically up‑regulated in response to cellular stress. HSP70 is a 72 kDa member of the heat shock protein 70 family of proteins. HSP70, also known as HSPA1A, HSP70-1, and HSP72 is a 641 amino acid (aa) heat shock protein. Over aa 1-641, human HSP70 shares 95% and 97% aa identity to mouse and rat HSP70.
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