|Other Names||Serine/threonine-protein kinase Sgk3, Cytokine-independent survival kinase, Serum/glucocorticoid-regulated kinase 3, Serum/glucocorticoid-regulated kinase-like, SGK3, CISK, SGKL|
|Target/Specificity||The synthetic peptide sequence is selected from aa 13~30 of human SGK3.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|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||Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, proliferation, survival and migration. Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. Plays a role in the regulation of renal tubular phosphate transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively regulates ER transcription activity through phosphorylation of FLII. Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes.|
|Cellular Location||Cytoplasmic vesicle. Early endosome. Recycling endosome. Note=Endosomal localization is a prerequisite for complete kinase activity. It is essential for its colocalization with the kinase responsible for phosphorylating Ser-486 thus allowing PDPK1 phosphorylation of Thr-320 resulting in complete activation of SGK3. Localized in vesicle-like structures and in the early endosome. Colocalizes with SLC9A3/NHE3 in the recycling endosomes|
|Tissue Location||Expressed in most tissues with highest levels in pancreas, kidney liver, heart and brain and lower levels in lung, placenta and skeletal muscle. Expression is higher in ER- positive breast tumors than ER-negative breast tumors|
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Provided below are standard protocols that you may find useful for product applications.
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein.By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. With more than 500 gene products, the protein kinase family is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. The AGC kinase group consists of 63 kinases including the cyclic nucleotide-regulated protein kinase (PKA & PKG) family, the diacylglycerol-activated/phospholipid-dependent protein kinase C (PKC) family, the related to PKA and PKC (RAC/Akt) protein kinase family, the kinases that phosphorylate G protein-coupled receptors family (ARK), and the kinases that phosphorylate ribosomal protein S6 family (RSK).The calcium/calmodulin-dependent kinase (CAMK) group consists of 75 kinases regulated by Ca2+/CaM and close relative family (CAMK, CAMKL, DAPK, MAPKAPK).
Blume-Jensen P, et al. Nature 2001. 411: 355.Cantrell D, J. Cell Sci. 2001. 114: 1439.Jhiang S Oncogene 2000. 19: 5590.Manning G, et al. Science 2002. 298: 1912.Moller, D, et al. Am. J. Physiol. 1994. 266: C351-C359.Robertson, S. et al. Trends Genet. 2000. 16: 368.Robinson D, et al. Oncogene 2000. 19: 5548.Van der Ven, P, et al. Hum. Molec. Genet. 1993. 2: 1889.Vanhaesebroeck, B, et al. Biochem. J. 2000. 346: 561.Van Weering D, et al. Recent Results Cancer Res. 1998. 154: 271.
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