TGF-α Detection (CAT#: STEM-MB-0250-WXH)

TGF-α, a transmembrane precursor protein, is cleaved by specific proteases, releases a soluble mature form containing an EGF-like domain. After binding to TGF-α, EGFR forms a dimer and the kinase domain is activated. Tyrosine phosphorylation of EGFR results in the recruitment of molecules with adapter or enzyme functions and activates downstream signaling pathways. The GRB2-associated son of sevenless (SOS) activates RAS by converting GDT to GTP. Active RAS recruits RAF kinases, which induces a series of kinase cascades, including phosphorylation of MEK1/2 and extracellular signal-regulated kinases 1/2 (ERK1/2). Activated ERK1/2 further phosphorylates a variety of cytosolic proteins and translocates them to the nucleus, thereby activating the expression of transcription factors such as c-fos and c-jun. This results in changes in cell gene expression, affecting cell behavior, such as proliferation, apoptosis, differentiation, and malignant transformation.

Study of epithelial cell proliferation, growth, and differentiation.
Study of tumor metastasis and invasion.

1. Process samples.
2. TGF-α detection (Enzyme-linked immunosorbent assay (ELISA), Flow cytometry).
3. Analysis results.

Sample Types-Blood, serum, plasma, cell culture supernatant, cell lysate, cell culture medium, tissue homogenate, urine, tumor, etc.