Detection of Human, Mouse, and Rat TSC1 by Western Blot.
Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line, PC3 human prostate cancer, Balb/3T3 mouse embryonic fibroblast cell line, and PC‑12 rat adrenal pheochromocytoma cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human/Mouse TSC1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4379) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for TSC1 at approximately 145 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
TSC1 (Tuberous sclerosis 1), or hamartin, is a tumor suppressor which interacts with tumor suppressor TSC2 (tuberin) to form a cytoplasmic heterodimer. Mutations in either hamartin or tuberin are responsible for tuberous sclerosis (TSC), an autosomal dominant disease characterized by renal dysfunction, seizures, developmental delays, benign hamartomas and low grade neoplasms predominantly affecting the CNS, kidney, lung, skin, and heart. The TSC1/TSC2 complex suppresses cell growth by inhibiting mTOR, with TSC1 acting to inhibit the ubiquitination of TSC2, leading to increased cellular levels of TSC2 and thus enhancing its catalytic activity as a GTPase-activating protein for Rheb. TSC1 and TSC2 are also involved in the G2/M transition of the cell cycle through their interactions with CDK1 and cyclin B1. TSC1 has also been shown to interact with F-actin and ERM (Ezrin-Radixin-Moesin) proteins, implying a role in the modulation of cell adhesion and morphology.
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