|Detection of Human/Mouse SCAMP3 by Western Blot. Western blot shows lysates of NIH‑3T3 mouse embryonic fibroblast cell line and K562 human chronic myelogenous leukemia cell line, HepG2 human hepatocellular carcinoma cell line, and JEG‑3 human epithelial choriocarcinoma cell line. PVDF membrane was probed with 1 µg/mL of Human/Mouse SCAMP3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5344) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for SCAMP3 at approximately 38 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
SCAMP3 (Secretory carrier membrane protein 3) is a 38‑40 kDa member of the SCAMP family of proteins. It is expressed in heart and skeletal muscle, plus fat, and functions in post-Golgi recycling and EGFR internalization pathways. Human SCAMP3 is 347 amino acids (aa) in length. It contains a cytoplasmic N-terminus (aa 1‑170) that shows three NPF repeats (binding sites for EH domain proteins), a heptad repeat of aliphatic aa's, and a potential SH3-binding motif. This is followed by four consecutive transmembrane domains (aa 171‑297) plus a C-terminal cytoplasmic region (aa 298‑347). It appears that phosphorylation of SCAMP3 on Tyr41 is a requisite for its interaction with EGFR. There are three potential splice forms. One shows a deletion of aa 23‑48, while two others show a one and 23 aa substitution for aa 131‑144 and 131‑260, respectively. Over aa 1‑170, human and mouse SCAMP3 are 91% aa identical.
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