rabbit anti-rapgef2  (AnaSpec)

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: The guanine nucleotide exchange factor RapGEF2 is required for ERK-dependent immediate-early gene (Egr1) activation during fear memory formation

doi: 10.1007/s00018-023-04999-y

Figure Lengend Snippet: Ablation of RapGEF2 protein expression in hippocampal CA1, DG and BLA. a Representative immunohistochemical images with RapGEF2 antibody (NNLE-2) for hippocampal subregions (CA1, DG and CA3) from flox and cKO mice at 5-weeks old (left panel) and 10 ~ 20 weeks old (right panel). Scale bar: 100 µm. b RapGEF2 immunoreactive (IR) signals in hippocampal CA1, DG and CA1 from cKO mice (10 ~ 20 weeks old) were quantified with NIH Image J and compared to RapGEF2 IR signals from flox mice. The result indicated a significant reduction in RapGEF2 levels in the CA1 and DG hippocampal subregions, but not in the CA3 subregion. N = 4 ~ 5 for animal number in each group. Student’s t-test for each region, **p < 0.001. c Western blots using protein lysates from hippocampal subregions of flox and cKO mice showed similar results that RapGEF2 was downregulated in CA1 and DG. N = 3 ~ 7 for animal number in each group, Student’s t-test for each region, **p < 0.001. d RapGEF2 immunoreactive (IR) signals in Amygdala from flox and cKO mice (10 ~ 20 weeks old) showed that RapGEF2 expression in BLA was significantly reduced in BLA, but not in CeA. Quantative assessment of RapGEF2 levels in BLA of wild-type and Camk2α-cre+/-::RapGEF2fl/fl mice has been previously reported (see Fig. 4B in [32])

Article Snippet: The primary antibodies used were rabbit anti-pERK (1:1500, Cell Signaling Technology, Danvers, MA), anti-c-Fos (1:5000, EnCor Biotechnology Inc., Gainesville, FL), anti-Egr-1 (15F7) (1:1000, Cell Signaling Technology, Danvers, MA) and rabbit anti-Rapgef2 (NNLE-2, custom-made by Anaspec [ 31 ]).

Techniques: Expressing, Immunohistochemical staining, Western Blot

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: The guanine nucleotide exchange factor RapGEF2 is required for ERK-dependent immediate-early gene (Egr1) activation during fear memory formation

doi: 10.1007/s00018-023-04999-y

Figure Lengend Snippet: Camk2α-cre+/-::RapGEF2fl/fl (cKO) mice show deficit in consolidation of contextual fear memory. a–f Consolidation of contextual fear memory was impaired in Camk2α-cre+/-::RapGEF2fl/fl mice. The scheme of a fear conditioning test used for cKO and flox control mice (a). cKO mice showed impaired contextual memory to the training context, not novel context, 24 h later compared to controls (b). However, both flox and cKO mice showed normal levels of freezing during the tone presentation in a non-training context when memory was retrieved 24 h after conditioning (c). Two-way ANOVA following by post hoc Bonferroni t-test, **p < 0.001. N = 22 for animal number of flox mice, N = 21 for animal number of cKO mice. Contextual freezing 3 h after the conditioning was similar between cKO and flox mice, suggesting acquisition and retrieval of memory was not affected in cKO mice (d). Two-way ANOVA following by post hoc Bonferroni t-test, **p < 0.001. N = 14 for animal number of flox mice, N = 18 for animal number of cKO mice. Flox and cKO mice showed similar freezing level immediately after foot-shock during fear conditioning (e, N = 36 for flox mouse number, 39 for cKO mouse number) and similar latency in a hot plate test (f, N = 19 ~ 26 for animal number in each group), suggesting no differences in pain sensitivity between two groups. g–k ERK activation in hippocampus during fear conditioning is RapGEF2-dependent. The Experimental procedure to examine ERK activation after fear conditioning (g). Representative images of phospho-ERK staining (in red) in hippocampal CA1 pyramidal cell layer (h, panels on the left) or hippocampal DG granule cell layer (i, panels on the left) of flox and cKO mice 10 min (FC10 min) or 30 min (FC 30 min) or 60 min (FC 60 min) after fear conditioning or without fear conditioning (NFC). Scale bar: 50 µm. Immunoreactive (IR) signals of phospho-ERK in the CA1 or DG of flox and cKO mice at different time points after fear conditioning were quantified by NIH Image J using the mean gray values of integrated density after being converted to gray scale; then compared to average value from mice in the home cage (NFC) to obtain “Relative IR of phospho-ERK” (h and i, panels on the right). N = 3 ~ 5 for animal number in each group. Two-way ANOVA following by post hoc Bonferroni t-test, *p < 0.05; **p < 0.001. Phospho-ERK activation in hippocampal CA1 and DG were also quantified with western blot (j and k). Hippocampal CA1 or DG were dissected out from flox or cKO mice 30 min post fear conditioning (FC) or without fear conditioning (NFC). Protein lysates were subjected to western blots with phospho-ERK, pan-ERK and GAPDH antibodies. N = 4 for animal number in each group. Protein bands from western blots were quantified using imageJ and GAPDH protein served as internal controls to normalize the loading. Phospho-ERK IR from different groups was compared to average value from flox mice in the home cage (NFC), to obtain “Relative IR of phospho-ERK”. Two-way ANOVA following by post hoc Bonferroni t-test, *p < 0.05; **p < 0.001

Article Snippet: The primary antibodies used were rabbit anti-pERK (1:1500, Cell Signaling Technology, Danvers, MA), anti-c-Fos (1:5000, EnCor Biotechnology Inc., Gainesville, FL), anti-Egr-1 (15F7) (1:1000, Cell Signaling Technology, Danvers, MA) and rabbit anti-Rapgef2 (NNLE-2, custom-made by Anaspec [ 31 ]).

Techniques: Hot Plate Test, Activation Assay, Staining, Western Blot

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: The guanine nucleotide exchange factor RapGEF2 is required for ERK-dependent immediate-early gene (Egr1) activation during fear memory formation

doi: 10.1007/s00018-023-04999-y

Figure Lengend Snippet: Differential dependency of RapGEF2 in fear conditioning-induced immediate early genes activation in hippocampal CA1 and DG. a Experimental procedure to examine IEGs activation after fear conditioning. b Representative images of cFos immunostaining in hippocampal CA1, DG and CA3 and basolateral amygdala of flox and cKO mice that were sacrificed 1 h after fear conditioning (FC) or stayed in the home cage (NFC). Scale bar: 200 µm. Lower panels are images with higher magnification of the boxed areas in the upper panels. c Quantification of cFos immunoreactivity in hippocampal subregions and basolateral amygdala of flox and cKO mice indicated that fear-conditioning induced cFos increase in all these regions. Immunoreactive (IR) signals for c-Fos from different brain areas as indicated were quantified by NIH Image J using the mean gray values of integrated density after being converted to gray scale. C-Fos IR from different groups was normalized to average value from flox mice in the home cage (NFC), to obtain “Relative IR of c-Fos”. No significant difference was observed between flox and cKO mice. N = 3 ~ 6 for animal number in each group. Two-way ANOVA followed by post hoc Bonferroni t-test, *p < 0.05, **p < 0.001. d Representative images of Egr-1 immunostaining in hippocampal CA1, DG and CA3 and basolateral amygdala of flox and cKO mice after fear conditioning. Scale bar: 200 µm. Lower panels are images with higher magnification of the boxed areas in the upper panels. e Quantification of Egr-1 immunoreactivity indicated that the fear-conditioning induced Egr-1 increase in CA1 and DG is RapGEF2-dependent. Immunoreactive (IR) signals for Egr-1 from different brain areas as indicated were quantified by NIH Image J using the mean gray values of integrated density after being converted to gray scale. Egr-1 IR from different groups was normalized to the average value for flox mice in the home cage (NFC), to obtain “Relative IR of Egr-1”. cKO mice with RapGEF2 ablation in CA1 and DG showed attenuated Egr-1 increase in CA1 and DG 1 h after fear conditioning, compared to flox mice. N = 3 ~ 6 for animal number in each group. Two-way ANOVA followed by post hoc Bonferroni t-test, *p < 0.05, **p < 0.001. f RNAscope with egr-1 (in red) and c-fos (in green) probes indicated that upregulation of c-fos mRNA in hippocampal CA1 and DG following fear conditioning occurred exclusively in the neurons with upregulation of egr-1 mRNA. Quantification of c-fos and egr-1 mRNA in hippocampal CA1 and DG 30 min after fear conditioning, 67.77% ± 10.92% of egr-1 positive neurons are cfos positive in CA1; 87.89% ± 7.67% of egr-1 positive neurons are cfos positive in DG. N = 3 for animal number in each group. Scale bar: 100 µm (left panels), 20 µm (right panels)

Article Snippet: The primary antibodies used were rabbit anti-pERK (1:1500, Cell Signaling Technology, Danvers, MA), anti-c-Fos (1:5000, EnCor Biotechnology Inc., Gainesville, FL), anti-Egr-1 (15F7) (1:1000, Cell Signaling Technology, Danvers, MA) and rabbit anti-Rapgef2 (NNLE-2, custom-made by Anaspec [ 31 ]).

Techniques: Activation Assay, Immunostaining

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: The guanine nucleotide exchange factor RapGEF2 is required for ERK-dependent immediate-early gene (Egr1) activation during fear memory formation

doi: 10.1007/s00018-023-04999-y

Figure Lengend Snippet: Differential dependency of RapGEF2 in immediate early gene activation in basolateral amygdala after fear conditioning with prior restraint stress. a and b Both contextual and cued fear memory was impaired in Camk2α-cre+/-::RapGEF2fl/fl mice (cKO) when 1 h restraint stress was applied 3 h prior to fear conditioning. Scheme of fear conditioning test employed is shown (a). cKO mice showed impaired contextual memory to the training context, not to a novel context, 24 h after conditioning, compared to controls (b, left panel). cKO mice showed attenuation in freezing during the tone presentation in a non-training context when memory was retrieved 24 h after conditioning (b, right panel). Two-way ANOVA followed by post hoc Bonferroni t-test, **p < 0.001, *p < 0.05. N = 23 flox mice, N = 18 cKO mice. c ERK activation in BLA after fear conditioning. pERK immunoreactivity (ir) in amygdala of RapGEF2fl/fl mice sacrificed at 15, 30, 60 min or 120 min after fear conditioning (FC15 min, FC 30 min, FC 60 min or FC 120 min) or from mice that stayed in home cage (NFC). Phospho-ERK IR in the BLA at different time points after fear conditioning was quantified using ImageJ, showing most prominent activation in BLA occurring 30–60 min after fear conditioning. N = 4 for animal number in each group. One-way ANOVA followed by post hoc Bonferroni t-test, *p < 0.05; **p < 0.001. Scale bar: 200 µm. d Experimental procedure to examine phospho-ERK and IEGs activation in BLA after fear conditioning without or with restraint stress. e ERK activation in the BLA of cKO mice 1 h after fear conditioning was not significantly different from that of flox mice. However, phospho-ERK IR level in the BLA was attenuated in cKO mice when acute restraint stress was applied prior to fear conditioning. N = 4 ~ 5 for animal number in each group. Two-way ANOVA followed by post hoc Bonferroni t-test, **p < 0.001. Scale bar: 200 µm. f Representative RNAscope images of cfos (green) and egr-1 (red) in basolateral amygdala of flox and cKO mice that were sacrificed 30 min or 1 h after fear conditioning with or without restraint stress. Scale bar: 200 µm (left panel), 50 µm (right panel). Upregulation of c-fos mRNA in BLA following fear conditioning occurred exclusively in the neurons with upregulation of egr-1 mRNA. Quantification of c-fos and egr-1 mRNA in BLA of flox mice 30 min after fear conditioning with or without restraint stress revealed that 12.62% ± 0.16% or 16.92 ± 2.70% of egr-1 positive neurons, respectively, are c-fos positive in BLA, N = 3 ~ 4 mice in each group. g cKO mice with RapGEF2 ablation in BLA showed attenuation in egr-1 mRNA, but not in c-fos mRNA increase in BLA after fear conditioning when acute restraint stress was applied prior to fear conditioning. Upregulation of c-fos mRNA in BLA following fear conditioning occurred only in the neurons with upregulation of egr-1 mRNA. C-fos and egr-1 mRNA signals were quantified by NIH Image J using the mean gray values of integrated density after being converted to gray scale; then normalized to average value from flox mice in the home cage (NFC) to obtain “Relative c-fos mRNA level” or “Relative egr-1 mRNA level”. N = 3 ~ 4 for animal number in each group. Two-way ANOVA followed by post hoc Bonferroni t-test, *p < 0.05, **p < 0.001

Article Snippet: The primary antibodies used were rabbit anti-pERK (1:1500, Cell Signaling Technology, Danvers, MA), anti-c-Fos (1:5000, EnCor Biotechnology Inc., Gainesville, FL), anti-Egr-1 (15F7) (1:1000, Cell Signaling Technology, Danvers, MA) and rabbit anti-Rapgef2 (NNLE-2, custom-made by Anaspec [ 31 ]).

Techniques: Activation Assay

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: RAPGEFs antibodies used in this study

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: Recombinant

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: Elevated levels of RAPGEF2 in the post‐mortem human AD hippocampus and AD mouse brains. A, Post‐mortem human hippocampal tissue from non‐patients (controls) and AD patients was subjected to western blot analysis for the RAPGEF2 levels. B, Quantification of RAPGEF2 levels normalised to GAPDH (control, n = 8; AD patients, n = 12). C, RAPGEF2 expression levels were analysed at 3 months of age in the hippocampus (HPC) and cortex (CTX) of wild‐type (WT) and 3xTg‐AD mice (TG). D, Quantification of RAPGEF2 levels in the HPC and CTX of 3‐month‐old WT ( n = 4; males), and TG mice ( n = 4; males). E, RAPGEF2 expression levels were analysed in the cortical lysates of 1.5‐month‐old WT and 5xFAD (TG) mice. Note that the levels of APP are markedly higher in the TG mice. F, Quantification of RAPGEF2 levels normalised to β‐actin ( n = 5; 4 males, 1 female). All data are shown as the mean ± SEM. ** p < 0.01, * p < 0.05; two‐tailed unpaired Student's t ‐test

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: Western Blot, Control, Expressing, Two Tailed Test

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: Oligomeric Aβ increases RAPGEF2 levels. A, SDS‐PAGE analysis of oligomeric Aβ. Oligomers were separated by western blotting on a 4%–12% gradient Bis‐Tris gel and immunoblotted with the 6E10 antibody. Oligomeric Aβ (AβO) consisted of monomers (~4 kDa), dimers, trimers, tetramers and high molecular weight (MW) oligomers. No fibrils (>75 kDa) were detected. B, Cultured cortical neurons (DIV 21) treated with vehicle or AβO (1 μM) for 6 h and immunoblotted for RAPGEF2. C, Relative fold change in RAPGEF2 levels ( n = 7). D, Representative RAPGEF2 fluorescence images of cultured hippocampal neurons. Neurons (DIV 21) treated with vehicle or oligomeric AβO (1 μM) for 6 h and immunolabelled for GFP and RAPGEF2. Scale, 100 μm. E, Quantification of the integrated intensity of RAPGEF2 in proximal dendrites ( n = 12). All data are shown as the mean ± SEM. * p < 0.05; two‐tailed unpaired Student's t ‐test

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: SDS Page, Western Blot, High Molecular Weight, Cell Culture, Fluorescence, Two Tailed Test

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: Knockdown of RAPGEF2 decreases JNK activation in 3xTg‐AD mice. A, Lentiviral particles expressing either shRAPGEF2 or a control vector (pll3.7) were transduced into cultured cortical neurons at DIV 7. After 8 days, cell culture lysates from wild‐type (WT) and 3xTg‐AD (TG) mice were used for western blot analysis of RAPGEF2 and MAPK levels ( n = 3). B–E, Quantification of RAPGEF2 (B), pJNK (C), pp38 (D), and pERK (E) levels. All data are shown as the mean ± SEM. * p < 0.05; Two‐way ANOVA, Tukey's multiple‐comparison test

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: Knockdown, Activation Assay, Expressing, Control, Plasmid Preparation, Cell Culture, Western Blot, Comparison

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: Knockdown of RAPGEF2 halts the AβO‐induced spine loss. A, Representative GFP fluorescence images of cultured hippocampal neurons. Neurons (DIV 18) were transfected with either scrambled shRNA or shRAPGEF2 for 3 days and treated with oligomeric Aβ (AβO, 1 μM) for 10 h before immunostaining. Bottom, Enlarged images of the data enclosed in rectangles at the top. Scale, 10 μm. B–D, Quantification of spine density (B), length (C), and head size (D) ( n = 12 neurons in scrambled‐vehicle and shRAPGEF2‐AβO; n = 13 neurons in shRAPGEF2‐vehicle and scrambled‐AβO). All data are shown as the mean ± SEM. * p < 0.05; ** p < 0.01, *** p < 0.001; one‐way ANOVA, Tukey's multiple‐comparison test

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: Knockdown, Fluorescence, Cell Culture, Transfection, shRNA, Immunostaining, Comparison

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: Knockdown of RAPGEF2 rescues fear memory deficits in 4‐month‐old 3xTg‐AD mice. A, Time course of stereotaxic delivery of lentiviral particles and behavioural tests. B, Representative image of GFP expression in the hippocampal CA1 area. Lentiviral particles simultaneously expressing shRAPGEF2 and GFP were bilaterally injected into the hippocampal CA1 area. Hoechst dye was used to stain neuronal nuclei (blue). Scale, 10 μm. Right, higher magnification image enclosed in rectangles at the left. A dotted line indicates the CA1 (mo: molecular layer in dentate gyrus). 53% ± 0.9% area of CA1 region was GFP‐positive (virus transduced) ( n = 3). Scale, 200 μm. C, Virus‐mediated knockdown extent of RAPGEF2 in vivo. Lentiviral particles expressing either shRAPGEF2 or a control empty vector (pll3.7) were transduced into hippocampal CA1 area in 2 months of wild‐type (WT) and 3xTg‐AD (TG) mice. After 2 months, hippocampal lysates were used for western blot analysis for RAPGEF2. APP‐FL (full length APP) were used as the marker of TG mice. D, Quantification of RAPGEF2 levels normalised to β‐Tubulin. pll3.7 in WT, n = 6 (5 males, 1 female); shRAPGEF2 in WT, n = 8 (7 males, 1 female); pll3.7 in TG, n = 4 (3 males, 1 female); shRAPGEF2 in TG, n = 8 (7 males, 1 female). E, The contextual fear memory test in 4‐month‐old wild‐type (WT) and 3xTg‐AD (TG) mice ( n = 6, males). F, Control (pll3.7) or shRAPGEF2‐expressing viral particles were injected into the hippocampal CA1 area in 2‐month‐old WT and 3xTg‐AD mice. After 2 months, the contextual fear memory test was performed (pll3.7 in WT, n = 15 males; shRAPGEF2 in WT, N = 8 males; pll3.7 in 3xTg‐AD mice, n = 22 males; shRAPGEF2 in 3xTg‐AD, n = 17 males). All data are shown as the mean ± SEM. * p < 0.05, ** p < 0.01; **** p < 0.0001; two‐tailed unpaired Student's t ‐test (E) and Two‐way ANOVA, Tukey's multiple‐comparison test (D and F)

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: Knockdown, Expressing, Injection, Staining, Virus, In Vivo, Control, Plasmid Preparation, Western Blot, Marker, Two Tailed Test, Comparison

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: Knockdown of RAPGEF2 preserves excitatory synapses in 3xTg‐AD mice. A, Representative electron microscopic images of the CA1 stratum radiatum of wild‐type (WT) and 3xTg‐AD mice injected with either control or shRAPGEF2‐expressing viral particles. The arrow indicates postsynaptic density. Scale, 1 μm. B, Representative images of asymmetric (left) and symmetric (right) synapses. The arrow indicates postsynaptic density. Scale, 0.5 μm. C and D, Quantification of the number of asymmetric (C) and symmetric (D) synapses for each condition. The data are shown as the mean ± SEM ( n = 95–97 images from three male mice per group). * p < 0.05, ** p < 0.01; Two‐way ANOVA, Tukey's multiple‐comparison test

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: Knockdown, Injection, Control, Expressing, Comparison

Journal: Neuropathology and Applied Neurobiology

Article Title: RAPGEF2 mediates oligomeric Aβ‐induced synaptic loss and cognitive dysfunction in the 3xTg‐AD mouse model of Alzheimer’s disease

doi: 10.1111/nan.12686

Figure Lengend Snippet: Schematic model for the role of RAPGEF2 in Aβ oligomer‐induced synaptic degeneration. In the AD hippocampus (right), synaptotoxic Aβ oligomers stimulate the upregulation of RAPGEF2 levels and lead to the activation of small GTPase Rap2. Rap2 activation, in turn, phosphorylates its downstream signalling target JNK. The Aβ oligomer‐mediated upregulation of RAPGEF2 induces the loss of excitatory synapses and subsequent memory impairment

Article Snippet: 2 , Rabbit polyclonal RAPGEF2 , A301‐966A , Bethyl Laboratories , 975–1025 amino acid of human RAPGEF2 (NP_055062.1, GeneID 9693).

Techniques: Activation Assay