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STK16 Antibody (clone M2)
Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E, RNAi |
|---|---|
| Primary Accession | O75716 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | Monoclonal |
| Clone Names | M2 |
| Calculated MW | 35kDa |
| Dilution | IHC-P (5 µg/ml) |
| Gene ID | 8576 |
|---|---|
| Other Names | Serine/threonine-protein kinase 16, 2.7.11.1, Myristoylated and palmitoylated serine/threonine-protein kinase, MPSK, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, Tyrosine-protein kinase STK16, 2.7.10.2, hPSK, STK16, MPSK1, PKL12, TSF1 |
| Reconstitution & Storage | Store at -20°C. Aliquot to avoid freeze/thaw cycles. |
| Precautions | STK16 Antibody (clone M2) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | STK16 |
|---|---|
| Synonyms | MPSK1, PKL12, TSF1 |
| Function | Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. |
| Cellular Location | Cytoplasm, perinuclear region. Membrane; Lipid-anchor. Note=Associates with Golgi and Golgi-derived vesicles. |
| Tissue Location | Ubiquitously expressed at very low levels. |
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Background
Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.
References
Ligos J.M.,et al.Biochem. Biophys. Res. Commun. 249:380-384(1998).
Berson A.E.,et al.Biochem. Biophys. Res. Commun. 259:533-538(1999).
Ohta S.,et al.Biochem. J. 350:395-404(2000).
Wabakken T.K.,et al.Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
Stairs D.B.,et al.Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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