Recombinant human SIK1 protein (Active) is a Human Fragment protein, in the 1 to 303 aa range, expressed in Baculovirus infected Sf9, with >80% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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. Inhibits CREB activity by phosphorylating and inhibiting activity of TORCs, the CREB-specific coactivators, like CRTC2/TORC2 and CRTC3/TORC3 in response to cAMP signaling (PubMed:29211348). 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 (By similarity).
SIK, SNF1LK, SIK1, Serine/threonine-protein kinase SIK1, Salt-inducible kinase 1, Serine/threonine-protein kinase SNF1-like kinase 1, SIK-1, Serine/threonine-protein kinase SNF1LK
Recombinant human SIK1 protein (Active) is a Human Fragment protein, in the 1 to 303 aa range, expressed in Baculovirus infected Sf9, with >80% purity and suitable for SDS-PAGE, FuncS.
pH: 7
Preservative: 1.02% Imidazole
Constituents: 25% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF
Affinity purified.
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. Inhibits CREB activity by phosphorylating and inhibiting activity of TORCs, the CREB-specific coactivators, like CRTC2/TORC2 and CRTC3/TORC3 in response to cAMP signaling (PubMed:29211348). 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 (By similarity).
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. AMPK subfamily.
Phosphorylated at Thr-182 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39, leading to its activation. Phosphorylation at Thr-182 promotes autophosphorylation at Ser-186, which is required for sustained activity. Autophosphorylation at Ser-186 is maintained by sequential phosphorylation at Thr-182 by GSK3-beta. GSK3-beta cannot initiate phosphorylation at Thr-182, it can only maintain it. Phosphorylation at Ser-575 in response to cAMP signaling promotes translocation to the cytoplasm (PubMed:29211348). Phosphorylation at Thr-322 by CaMK1 following intracellular sodium concentration leads to activation.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
SIK1 also known as salt-inducible kinase 1 functions as a serine/threonine-protein kinase. This protein has a mass of approximately 85 kDa. SIK1 expression occurs in multiple tissues with high levels found in the brain and cardiac muscle. Mechanically SIK1 phosphorylates a variety of substrates which modifies their activity or stability. By adding phosphate groups to specific sequences it alters protein functions and cellular pathways impacting cellular processes like metabolism and transcription.
Salt-inducible kinase 1 plays an important role in regulating cellular responses to metabolic stress and hormonal signaling. It forms part of a kinase complex where it operates alongside other kinases and regulatory proteins to modulate gene expression and metabolic pathways. SIK1 influences gluconeogenesis and lipogenesis processes essential for maintaining energy homeostasis. The regulation by SIK1 of these processes is essential to adapt to changes in cellular environment and energy requirements.
Salt-inducible kinase 1 is an important regulator within the cAMP signaling pathway and the AMPK signaling pathway. In the cAMP pathway SIK1 interacts with protein kinase A (PKA) contributing to the modulation of the transcription factor CREB. In the AMPK pathway SIK1 indirectly affects energy balance by influencing downstream genes involved in glucose production and fatty acid metabolism. These interactions highlight SIK1's place in controlling energy and metabolic homeostasis in response to external stimuli.
Salt-inducible kinase 1 has been linked to conditions such as cardiac hypertrophy and type 2 diabetes. In cardiac hypertrophy SIK1 affects the remodeling of cardiac tissue potentially interacting with the protein HDAC which is important in regulating cardiac muscle gene expression. In type 2 diabetes the altered activity or expression of SIK1 could disrupt normal glucose metabolism while pathways involving proteins like AMPK may contribute to insulin resistance. Understanding these relationships can aid in developing therapeutic strategies targeting SIK1-related pathways.
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The specific activity of ab268969 was 290 nmol/min/mg in a kinase assay using AMARA synthetic peptide (AMARAASAAALARRR) as substrate.
SDS-PAGE analysis of ab268969.
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