|Application ||WB, E|
|Other Accession||Q9R1U5, NP_034961.2|
|Calculated MW||85115 Da|
|Antigen Region||573-600 aa|
|Other Names||Serine/threonine-protein kinase SIK1, HRT-20, Myocardial SNF1-like kinase, Salt-inducible kinase 1, SIK-1, Serine/threonine-protein kinase SNF1-like kinase 1, Serine/threonine-protein kinase SNF1LK, Sik1, Msk, Sik, Snf1lk|
|Target/Specificity||This Sik1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 573-600 amino acids from the C-terminal region of mouse Sik1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Sik1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||Msk, Sik, Snf1lk|
|Function||Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1.|
|Cellular Location||Cytoplasm. Nucleus. Note=Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ|
|Tissue Location||Expressed in lung, skin, ovary, heart and stomach. No expression in brain, liver or adult skeletal muscle but is present in skeletal muscle progenitor cells of the somite beginning at 9.5 dpc. Present at 8.0 dpc in the monolayer of presumptive myocardial cells but rapidly down-regulated at 8.5 dpc upon primitive ventricle formation, although still present in myocardial cells that will populate the primitive atrium and bulbus cordis. At 9.5 dpc expression is down-regulated in the primitive atrium but observed in the sinus venosus and truncus arteriosus.|
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Provided below are standard protocols that you may find useful for product applications.
Transient role during the earliest stages of myocardial cell differentiation and/or primitive chamber formation and may also be important for the earliest stages of skeletal muscle growth and/or differentiation. Potential role in G2/M cell cycle regulation. Inhibits CREB activity by phosphorylating and repressing the CREB-specific coactivators, CRTC1-3.
Romito, A., et al. PLoS ONE 5 (2), E9029 (2010) :
Takemori, H., et al. Endocr. J. 56(1):121-130(2009)
Berdeaux, R., et al. Nat. Med. 13(5):597-603(2007)
Katoh, Y., et al. FEBS J. 273(12):2730-2748(2006)
Cobellis, G., et al. Nucleic Acids Res. 33 (4), E44 (2005) :
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