|Other Names||SCY1-like protein 2, Coated vesicle-associated kinase of 104 kDa, SCYL2, CVAK104, KIAA1360|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7024b was selected from the C-term region of human SCYL2 (C-term). A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. According to PubMed:15809293, probable serine/threonine-protein kinase that phosphorylates, in vitro, the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L- lysine. According to PubMed:16914521, has no detectable kinase activity in vitro. May regulate clathrin-dependent trafficking between the TGN and/or the endosomal system.|
|Cellular Location||Cytoplasm, perinuclear region. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network membrane. Endosome membrane. Note=According to PubMed:15809293, plasma membrane-associated in clathrin-coated vesicles. According to PubMed:16914521, colocalizes to the trans- Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes|
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Provided below are standard protocols that you may find useful for product applications.
SCYL2 is a component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. SCYL2 is a probable serine/threonine-protein kinase that phosphorylates, in vitro, the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L-lysine. SCYL2 may also regulate clathrin-dependent trafficking between the TGN and/or the endosomal system.
Ota, T., et al., Nat. Genet. 36(1):40-45 (2004).
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