Recombinant Human Serum/Glucocorticoid Regulated Kinase 1, His-tagged

Cat.No. : SGK1-1346H
Product Overview : Recombinant human SGK1 protein was expressed with N-terminal His-tag in High-Five cells using baculovirus expression system and purified by using conventional chromatography techniques. MW: 44.5 kDa.
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Species : Human
Source : Hi-5 Insect Cells
Tag : His
Protein Length : 60-431aa
Description : SGK1 is a serine/threonine protein kinase and a member of the AGC subfamily, which includes protein kinases A, G, and C. This protein plays an important role in activating certain potassium, sodium and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion.
Form : Liquid. 20mM Tris-HCl buffer (pH8.0) containing 30% glycerol 0.2M NaCl,2mM DTT,0.1mM PMSF.
Molecular Mass : 44.5 kDa (393aa)
AA Sequence : MGSSHHHHHH SSGLVPRGSH MISQPQEPEL MNANPSPPPS PSQQINLGPS SNPHAKPSDF HFLKVIGKGS FGKVLLARHK AEEVFYAVKV LQKKAILKKK EEKHIMSERN VLLKNVKHPF LVGLHFSFQT ADKLYFVLDY INGGELFYHL QRERCFLEPR ARFYAAEIAS ALGYLHSLNI VYRDLKPENI LLDSQGHIVL TDFGLCKENI EHNSTTSTFC GTPEYLAPEV LHKQPYDRTV DWWCLGAVLY EMLYGLPPFY SRNTAEMYDN ILNKPLQLKP NITNSARHLL EGLLQKDRTK RLGAKDDFME IKSHVFFSLI NWDDLINKKI TPPFNPNVSG PNDLRHFDPE FTEEPVPNSI GKSPDSVLVT ASVKEAAEAF LGFSYAPPTD SFL
Purity : >90% by SDS - PAGE
Applications : SDS-PAGE
Storage : Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.
Concentration : 0.25 mg/ml (determined by Bradford assay)
Gene Name SGK1 serum/glucocorticoid regulated kinase 1 [ Homo sapiens ]
Official Symbol SGK1
Synonyms SGK1; serum/glucocorticoid regulated kinase 1; serum/glucocorticoid regulated kinase , SGK; serine/threonine-protein kinase Sgk1; serine/threonine protein kinase SGK; serum/glucocorticoid-regulated kinase 1; SGK;
Gene ID 6446
mRNA Refseq NM_001143676
Protein Refseq NP_001137148
MIM 602958
UniProt ID O00141
Chromosome Location 6q23
Pathway Aldosterone-regulated sodium reabsorption, organism-specific biosystem; Aldosterone-regulated sodium reabsorption, conserved biosystem; Class I PI3K signaling events, organism-specific biosystem; FoxO family signaling, organism-specific biosystem; Glucocorticoid receptor regulatory network, organism-specific biosystem; IL-6 Signaling Pathway, organism-specific biosystem; Insulin Pathway, organism-specific biosystem;
Function ATP binding; calcium channel regulator activity; chloride channel regulator activity; nucleotide binding; potassium channel regulator activity; protein serine/threonine kinase activity; sodium channel regulator activity;

The Bromodomain Protein 4 Contributes to the Regulation of Alternative Splicing

Journal: Cell reports    PubMed ID: 31747612    Data: 2019/12/5

Authors: Sheetal Uppal, Anne Gegonne, Dinah S. Singer

Article Snippet:(+)- JQ1 , BPS Bioscience , 27400.(+)- JQ1 , BPS Bioscience , 27400.. Recombinant Human HNRNPM protein, His-tagged , Creative BioMart , 5432H.. Glutathione Agarose beads , Thermo Scientific , 16100.Glutathione Agarose beads , Thermo Scientific , 16100.

(A) Immunoblot of BRD4 immunoprecipitates from thymocyte nuclear extracts (with and without benzonase treatment) with indicated antibodies to splicing factors FUS, HnRNPL, and U1–70. The immunoprecipitates from a single extract were run on either a 6% gel to visualize BRD4 and Fus or on a 10% gel to visualize HnRNPL and U1–70. The values under the IP lanes indicate the enrichment of anti-BRD4 co-IP, relative to the IgG control. (B, left) Immunoblot of BRD4 immunoprecipitates from HeLa nuclear extracts with indicated antibodies to splicing factors FUS, HnRNPM, U1–70, and U1-A. (B, right) Immunoblot of FUS immunoprecipitates from HeLa nuclear extracts with indicated antibodies to BRD4 and splicing factors HnRNPM, U1–70, and U1-A. (C) Schematic representation of BRD4 and BRD4-deletion mutants. The coordinates of the mouse BRD4 mutations are as follows. WT BRD4, 1402 aa; DN, 722–1402 aa; ΔC, 1–699aa; ΔBD1, 146–1402 aa; ΔBD2+B, 1–349/599–1402 aa; ΔB, 1–502/549–1402 aa; ΔET, 1–600/684–1402 aa; ΔHAT, 1–1156/1198–1402 aa. (D) Immunoblots showing pull-down analysis of recombinant BRD4 with recombinant HnRNPM. rHnRNPM (0.25 μg) was pulled down with rflag-BRD4 (0.5 μg) immobilized on Flag beads. Immunoblots were with anti-HnRNPM (upper) and anti-BRD4 (lower). (E) Immunoblots showing pull-down analysis of recombinant BRD4 with recombinant FUS. rFUS (0.25 μg) was pulled down with rflag-BRD4 (0.5 μg) WT or equimolar amounts of N-terminal or C-terminal BRD4 truncation mutants immobilized on Flag beads. Immunoblots were with anti-FUS (upper) and anti-BRD4 (lower). (F) Binding of HnRNPM (left panel) and FUS (right panel) to BRD4 mutants was assessed in pull-down assays with rBRD4 immobilized on Flag beads and immunoblotting with appropriate antibodies. The results represent the average of two experiments. (G) Retention of FUS and HnRNPM to BRD4 mutants, relative to the WT, was quantified as the fraction of input and normalized to the extent of binding to BRD4 WT. All results are representative of at least two independent experiments. See also Figure S5.

(A) Immunoblot of BRD4 immunoprecipitates from thymocyte nuclear extracts (with and without benzonase treatment) with indicated antibodies to splicing factors FUS, HnRNPL, and U1–70. The immunoprecipitates from a single extract were run on either a 6% gel to visualize BRD4 and Fus or on a 10% gel to visualize HnRNPL and U1–70. The values under the IP lanes indicate the enrichment of anti-BRD4 co-IP, relative to the IgG control. (B, left) Immunoblot of BRD4 immunoprecipitates from HeLa nuclear extracts with indicated antibodies to splicing factors FUS, HnRNPM, U1–70, and U1-A. (B, right) Immunoblot of FUS immunoprecipitates from HeLa nuclear extracts with indicated antibodies to BRD4 and splicing factors HnRNPM, U1–70, and U1-A. (C) Schematic representation of BRD4 and BRD4-deletion mutants. The coordinates of the mouse BRD4 mutations are as follows. WT BRD4, 1402 aa; DN, 722–1402 aa; ΔC, 1–699aa; ΔBD1, 146–1402 aa; ΔBD2+B, 1–349/599–1402 aa; ΔB, 1–502/549–1402 aa; ΔET, 1–600/684–1402 aa; ΔHAT, 1–1156/1198–1402 aa. (D) Immunoblots showing pull-down analysis of recombinant BRD4 with recombinant HnRNPM. rHnRNPM (0.25 μg) was pulled down with rflag-BRD4 (0.5 μg) immobilized on Flag beads. Immunoblots were with anti-HnRNPM (upper) and anti-BRD4 (lower). (E) Immunoblots showing pull-down analysis of recombinant BRD4 with recombinant FUS. rFUS (0.25 μg) was pulled down with rflag-BRD4 (0.5 μg) WT or equimolar amounts of N-terminal or C-terminal BRD4 truncation mutants immobilized on Flag beads. Immunoblots were with anti-FUS (upper) and anti-BRD4 (lower). (F) Binding of HnRNPM (left panel) and FUS (right panel) to BRD4 mutants was assessed in pull-down assays with rBRD4 immobilized on Flag beads and immunoblotting with appropriate antibodies. The results represent the average of two experiments. (G) Retention of FUS and HnRNPM to BRD4 mutants, relative to the WT, was quantified as the fraction of input and normalized to the extent of binding to BRD4 WT. All results are representative of at least two independent experiments. See also Figure S5.

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