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from Acdp1 N- (TSFLLRVYFQPGPPATAAPVPSPT) and C- (TQQLTLSPAAVPTR) terminuses, conserved peptide from ACD domain of Acdp1 (HNIVDILFVKDLAFVDPDDCTPLLTVTRF) were commercially synthesized (Sigma Genosys). These antigenic sites were predicted by software from Sigma Genosys and polyclonal antibodies for each peptide were produced by immunizing rabbits. To test the specificity of the antibodies, we conducted Western-blot analysis of mouse brain tissue extracts. As shown in Fig. 6A, the antibody produced by C-terminal peptide specifically detected Acdp1 (lane 3). The antibody generated by N-terminal peptide recognized Acdp4 in addition to Acdp1, although the reactivity to latter was significantly higher (Fig. 6A, lane 2). As expected, the antibody produced by the conserved sequence peptide detected all Acdp proteins (Fig. 6A, lane 1). To further determine the specificity of the antibody against the Acdp1 C-terminus, we analyzed extracts of HEK293, 3T3 and PC12 cells. The results are shown in Fig. 6B. Apparently, this antibody detected a specific band of Acdp1 in all cell lysates. Of note, shown in Fig. 6B are signals of 10 μg extracts of HEK293 cell lysates, 100 μg extracts of 3T3 and PC12 cell lysates. Thus, the expression levels of Acdp1 in these cell types vary a lot, with the highest expression in HEK293 cells. Nevertheless, these immunoblot results support our analysis of brain tissue extracts that the antibody against Acdp1 C-terminus specifically recognizes Acdp-1."}

{"project":"craft-ca-core-dev","denotations":[{"id":"T2726","span":{"begin":214,"end":223},"obj":"CHEBI:59132"},{"id":"T2725","span":{"begin":123,"end":128},"obj":"PR:000005643"},{"id":"T2724","span":{"begin":113,"end":119},"obj":"SO:0000417"},{"id":"T2723","span":{"begin":14,"end":19},"obj":"PR:000005643"},{"id":"T2750","span":{"begin":1488,"end":1494},"obj":"PR:000005643"},{"id":"T2749","span":{"begin":1447,"end":1452},"obj":"PR:000005643"},{"id":"T2748","span":{"begin":1430,"end":1438},"obj":"GO:0042571"},{"id":"T2747","span":{"begin":1405,"end":1411},"obj":"UBERON:0000479"},{"id":"T2746","span":{"begin":1399,"end":1404},"obj":"UBERON:0000955"},{"id":"T2745","span":{"begin":1308,"end":1318},"obj":"GO:0010467"},{"id":"T2744","span":{"begin":1253,"end":1258},"obj":"PR:000005643"},{"id":"T2743","span":{"begin":1232,"end":1242},"obj":"GO:0010467"},{"id":"T2742","span":{"begin":1069,"end":1074},"obj":"PR:000005643"},{"id":"T2741","span":{"begin":1032,"end":1040},"obj":"GO:0042571"},{"id":"T2740","span":{"begin":911,"end":916},"obj":"PR:000005643"},{"id":"T2739","span":{"begin":890,"end":898},"obj":"GO:0042571"},{"id":"T2738","span":{"begin":748,"end":756},"obj":"GO:0042571"},{"id":"T2737","span":{"begin":646,"end":651},"obj":"PR:000005643"},{"id":"T2736","span":{"begin":625,"end":630},"obj":"PR:000005646"},{"id":"T2735","span":{"begin":573,"end":581},"obj":"GO:0042571"},{"id":"T2734","span":{"begin":553,"end":558},"obj":"PR:000005643"},{"id":"T2733","span":{"begin":491,"end":499},"obj":"GO:0042571"},{"id":"T2732","span":{"begin":449,"end":455},"obj":"UBERON:0000479"},{"id":"T2731","span":{"begin":443,"end":448},"obj":"UBERON:0000955"},{"id":"T2730","span":{"begin":437,"end":442},"obj":"NCBITaxon:10088"},{"id":"T2729","span":{"begin":387,"end":397},"obj":"GO:0042571"},{"id":"T2728","span":{"begin":347,"end":354},"obj":"NCBITaxon:9986"},{"id":"T2727","span":{"begin":291,"end":301},"obj":"GO:0042571"}],"text":"Peptides from Acdp1 N- (TSFLLRVYFQPGPPATAAPVPSPT) and C- (TQQLTLSPAAVPTR) terminuses, conserved peptide from ACD domain of Acdp1 (HNIVDILFVKDLAFVDPDDCTPLLTVTRF) were commercially synthesized (Sigma Genosys). These antigenic sites were predicted by software from Sigma Genosys and polyclonal antibodies for each peptide were produced by immunizing rabbits. To test the specificity of the antibodies, we conducted Western-blot analysis of mouse brain tissue extracts. As shown in Fig. 6A, the antibody produced by C-terminal peptide specifically detected Acdp1 (lane 3). The antibody generated by N-terminal peptide recognized Acdp4 in addition to Acdp1, although the reactivity to latter was significantly higher (Fig. 6A, lane 2). As expected, the antibody produced by the conserved sequence peptide detected all Acdp proteins (Fig. 6A, lane 1). To further determine the specificity of the antibody against the Acdp1 C-terminus, we analyzed extracts of HEK293, 3T3 and PC12 cells. The results are shown in Fig. 6B. Apparently, this antibody detected a specific band of Acdp1 in all cell lysates. Of note, shown in Fig. 6B are signals of 10 μg extracts of HEK293 cell lysates, 100 μg extracts of 3T3 and PC12 cell lysates. Thus, the expression levels of Acdp1 in these cell types vary a lot, with the highest expression in HEK293 cells. Nevertheless, these immunoblot results support our analysis of brain tissue extracts that the antibody against Acdp1 C-terminus specifically recognizes Acdp-1."}

{"project":"craft-ca-core-ex-dev","denotations":[{"id":"T2829","span":{"begin":1488,"end":1494},"obj":"PR_EXT:000005643"},{"id":"T2828","span":{"begin":1453,"end":1463},"obj":"CHEBI_SO_EXT:C_terminus_or_C_terminal_region"},{"id":"T2827","span":{"begin":1447,"end":1452},"obj":"PR_EXT:000005643"},{"id":"T2826","span":{"begin":1430,"end":1438},"obj":"GO:0042571"},{"id":"T2825","span":{"begin":1405,"end":1411},"obj":"UBERON:0000479"},{"id":"T2824","span":{"begin":1399,"end":1404},"obj":"UBERON:0000955"},{"id":"T2823","span":{"begin":1329,"end":1334},"obj":"CL_GO_EXT:cell"},{"id":"T2822","span":{"begin":1308,"end":1318},"obj":"GO:0010467"},{"id":"T2821","span":{"begin":1268,"end":1272},"obj":"CL_GO_EXT:cell"},{"id":"T2820","span":{"begin":1253,"end":1258},"obj":"PR_EXT:000005643"},{"id":"T2819","span":{"begin":1232,"end":1242},"obj":"GO:0010467"},{"id":"T2818","span":{"begin":1208,"end":1212},"obj":"CL_GO_EXT:cell"},{"id":"T2817","span":{"begin":1162,"end":1166},"obj":"CL_GO_EXT:cell"},{"id":"T2816","span":{"begin":1082,"end":1086},"obj":"CL_GO_EXT:cell"},{"id":"T2815","span":{"begin":1069,"end":1074},"obj":"PR_EXT:000005643"},{"id":"T2814","span":{"begin":1032,"end":1040},"obj":"GO:0042571"},{"id":"T2813","span":{"begin":974,"end":979},"obj":"CL_GO_EXT:cell"},{"id":"T2812","span":{"begin":917,"end":927},"obj":"CHEBI_SO_EXT:C_terminus_or_C_terminal_region"},{"id":"T2811","span":{"begin":911,"end":916},"obj":"PR_EXT:000005643"},{"id":"T2810","span":{"begin":890,"end":898},"obj":"GO:0042571"},{"id":"T2809","span":{"begin":818,"end":826},"obj":"CHEBI_PR_EXT:protein"},{"id":"T2808","span":{"begin":813,"end":817},"obj":"PR_EXT:ACDP_or_CNNM"},{"id":"T2807","span":{"begin":792,"end":799},"obj":"CHEBI_SO_EXT:peptide_or_peptide_region"},{"id":"T2806","span":{"begin":783,"end":791},"obj":"SO_EXT:biological_sequence"},{"id":"T2805","span":{"begin":773,"end":782},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T2804","span":{"begin":748,"end":756},"obj":"GO:0042571"},{"id":"T2803","span":{"begin":646,"end":651},"obj":"PR_EXT:000005643"},{"id":"T2802","span":{"begin":625,"end":630},"obj":"PR_EXT:000005646"},{"id":"T2801","span":{"begin":606,"end":613},"obj":"CHEBI_SO_EXT:peptide_or_peptide_region"},{"id":"T2800","span":{"begin":595,"end":605},"obj":"CHEBI_SO_EXT:N_terminus_or_N_terminal_region"},{"id":"T2799","span":{"begin":573,"end":581},"obj":"GO:0042571"},{"id":"T2798","span":{"begin":553,"end":558},"obj":"PR_EXT:000005643"},{"id":"T2797","span":{"begin":523,"end":530},"obj":"CHEBI_SO_EXT:peptide_or_peptide_region"},{"id":"T2796","span":{"begin":512,"end":522},"obj":"CHEBI_SO_EXT:C_terminus_or_C_terminal_region"},{"id":"T2795","span":{"begin":491,"end":499},"obj":"GO:0042571"},{"id":"T2794","span":{"begin":449,"end":455},"obj":"UBERON:0000479"},{"id":"T2793","span":{"begin":443,"end":448},"obj":"UBERON:0000955"},{"id":"T2792","span":{"begin":437,"end":442},"obj":"NCBITaxon:10088"},{"id":"T2791","span":{"begin":387,"end":397},"obj":"GO:0042571"},{"id":"T2790","span":{"begin":347,"end":354},"obj":"NCBITaxon:9986"},{"id":"T2789","span":{"begin":311,"end":318},"obj":"CHEBI_SO_EXT:peptide_or_peptide_region"},{"id":"T2788","span":{"begin":291,"end":301},"obj":"GO:0042571"},{"id":"T2787","span":{"begin":214,"end":223},"obj":"CHEBI_EXT:59132"},{"id":"T2786","span":{"begin":123,"end":128},"obj":"PR_EXT:000005643"},{"id":"T2785","span":{"begin":113,"end":119},"obj":"SO_EXT:0000417"},{"id":"T2784","span":{"begin":96,"end":103},"obj":"CHEBI_SO_EXT:peptide_or_peptide_region"},{"id":"T2783","span":{"begin":86,"end":95},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T2782","span":{"begin":74,"end":84},"obj":"CHEBI_SO_EXT:C_terminus_or_C_terminal_region"},{"id":"T2781","span":{"begin":54,"end":56},"obj":"_FRAGMENT"},{"id":"T2780","span":{"begin":74,"end":84},"obj":"CHEBI_SO_EXT:N_terminus_or_N_terminal_region"},{"id":"T2779","span":{"begin":20,"end":22},"obj":"_FRAGMENT"},{"id":"T2778","span":{"begin":14,"end":19},"obj":"PR_EXT:000005643"},{"id":"T2777","span":{"begin":0,"end":8},"obj":"CHEBI_SO_EXT:peptide_or_peptide_region"}],"relations":[{"id":"R1570","pred":"_lexicallyChainedTo","subj":"T2780","obj":"T2779"},{"id":"R1571","pred":"_lexicallyChainedTo","subj":"T2782","obj":"T2781"}],"text":"Peptides from Acdp1 N- (TSFLLRVYFQPGPPATAAPVPSPT) and C- (TQQLTLSPAAVPTR) terminuses, conserved peptide from ACD domain of Acdp1 (HNIVDILFVKDLAFVDPDDCTPLLTVTRF) were commercially synthesized (Sigma Genosys). These antigenic sites were predicted by software from Sigma Genosys and polyclonal antibodies for each peptide were produced by immunizing rabbits. To test the specificity of the antibodies, we conducted Western-blot analysis of mouse brain tissue extracts. As shown in Fig. 6A, the antibody produced by C-terminal peptide specifically detected Acdp1 (lane 3). The antibody generated by N-terminal peptide recognized Acdp4 in addition to Acdp1, although the reactivity to latter was significantly higher (Fig. 6A, lane 2). As expected, the antibody produced by the conserved sequence peptide detected all Acdp proteins (Fig. 6A, lane 1). To further determine the specificity of the antibody against the Acdp1 C-terminus, we analyzed extracts of HEK293, 3T3 and PC12 cells. The results are shown in Fig. 6B. Apparently, this antibody detected a specific band of Acdp1 in all cell lysates. Of note, shown in Fig. 6B are signals of 10 μg extracts of HEK293 cell lysates, 100 μg extracts of 3T3 and PC12 cell lysates. Thus, the expression levels of Acdp1 in these cell types vary a lot, with the highest expression in HEK293 cells. Nevertheless, these immunoblot results support our analysis of brain tissue extracts that the antibody against Acdp1 C-terminus specifically recognizes Acdp-1."}