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>   home   >   Products   >   Peptides   >   Blocking Peptides   >   Arhgef9 Antibody (Center) Blocking Peptide   

Arhgef9 Antibody (Center) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession Q9QX73
Clone Names 5120572
Additional Information
Other Names Rho guanine nucleotide exchange factor 9, Collybistin, Rac/Cdc42 guanine nucleotide exchange factor 9, Arhgef9
Target/Specificity The synthetic peptide sequence used to generate the antibody AP2713c was selected from the Center region of human Arhgef9. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name Arhgef9
Function Acts as guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters.
Cellular Location Cytoplasm. Cell junction, synapse, postsynaptic density {ECO:0000250|UniProtKB:Q3UTH8}
Tissue Location Detected in brain, throughout the gray matter. Detected at low levels in heart and skeletal muscle EMBL; AJ250425; CAB65966.1; -; mRNA EMBL; AJ302676; CAC16410.1; -; mRNA RefSeq; NP_076447.1; NM_023957.1. [Q9QX73-1] PDB; 2DFK; X-ray; 2.15 A; A/C=71-463 PDB; 4MT6; X-ray; 5.50 A; A=1-456 PDB; 4MT7; X-ray; 3.50 A; A=10-493 PDBsum; 2DFK; - PDBsum; 4MT6; - PDBsum; 4MT7; - SMR; Q9QX73; - PhosphoSitePlus; Q9QX73; - PaxDb; Q9QX73; - PRIDE; Q9QX73; - GeneID; 66013; - KEGG; rno:66013; - CTD; 23229; - RGD; 620719; Arhgef9 InParanoid; Q9QX73; - KO; K20686; - OrthoDB; 428887at2759; - PhylomeDB; Q9QX73; - Reactome; R-RNO-193648; NRAGE signals death through JNK Reactome; R-RNO-194840; Rho GTPase cycle Reactome; R-RNO-416482; G alpha (12/13) signalling events Reactome; R-RNO-977443; GABA receptor activation EvolutionaryTrace; Q9QX73; - PRO; PR:Q9QX73; - Proteomes; UP000002494; Unplaced GO; GO:0005938; C:cell cortex; IDA:RGD GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO GO; GO:0098690; C:glycinergic synapse; IDA:SynGO GO; GO:0005886; C:plasma membrane; IEA:GOC GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB GO; GO:0099572; C:postsynaptic specialization; IDA:SynGO GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW GO; GO:0043113; P:receptor clustering; IDA:RGD GO; GO:0099150; P:regulation of postsynaptic specialization assembly; ISO:RGD CDD; cd00160; RhoGEF; 1 CDD; cd11975; SH3_ARHGEF9; 1 Gene3D; 1.20.900.10; -; 1 Gene3D;; -; 1 IDEAL; IID50103; - InterPro; IPR035728; ARHGEF9_SH3 InterPro; IPR035899; DBL_dom_sf InterPro; IPR000219; DH-domain InterPro; IPR011993; PH-like_dom_sf InterPro; IPR001849; PH_domain InterPro; IPR036028; SH3-like_dom_sf InterPro; IPR001452; SH3_domain Pfam; PF00169; PH; 1 Pfam; PF00621; RhoGEF; 1 Pfam; PF00018; SH3_1; 1 SMART; SM00233; PH; 1 SMART; SM00325; RhoGEF; 1 SMART; SM00326; SH3; 1 SUPFAM; SSF48065; SSF48065; 1 SUPFAM; SSF50044; SSF50044; 1 PROSITE; PS50010; DH_2; 1 PROSITE; PS50003; PH_DOMAIN; 1 PROSITE; PS50002; SH3; 1 1: Evidence at protein level; 3D-structure; Alternative splicing; Cell junction; Cytoplasm; Guanine-nucleotide releasing factor; Reference proteome; SH3 domain; Synapse CHAIN 1..493 /note="Rho guanine nucleotide exchange factor 9" /id="PRO_0000253898" DOMAIN 15..74 /note="SH3" /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" DOMAIN 110..294 /note="DH" /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" DOMAIN 325..432 /note="PH" /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" REGION 107..117 /note="Interaction with GPHN" VAR_SEQ 12..71 /note="Missing (in isoform 2)" /evidence="ECO:0000303|PubMed:10607391" /id="VSP_021147" VAR_SEQ 464..493 /note="GRVGEEENQSLELKRACEVLQRLWSPGKKS -> VTQRKWHY (in isoform 2)" /evidence="ECO:0000303|PubMed:10607391" /id="VSP_021148" MUTAGEN 107 /note="R->A: No effect on formation of GPHN clusters; when associated with A-108 and A-117." /evidence="ECO:0000269|PubMed:11727829, ECO:0000269|PubMed:16616186" MUTAGEN 108 /note="D->A: No effect on GPHN clusters; when associated with A-107 and A-117." /evidence="ECO:0000269|PubMed:11727829, ECO:0000269|PubMed:16616186" MUTAGEN 111 /note="R->A: Loss of formation of GPHN clusters." /evidence="ECO:0000269|PubMed:11727829, ECO:0000269|PubMed:16616186" MUTAGEN 117 /note="E->A: No effect on GPHN clusters; when associated with A-107 and A-108." /evidence="ECO:0000269|PubMed:11727829, ECO:0000269|PubMed:16616186" MUTAGEN 297 /note="R->H: Defects in binding to phosphatidylinositol-3- phosphate and in formation of GPHN clusters." /evidence="ECO:0000269|PubMed:25678704" HELIX 107..135 /evidence="ECO:0000244|PDB:2DFK" HELIX 137..142 /evidence="ECO:0000244|PDB:2DFK" TURN 144..146 /evidence="ECO:0000244|PDB:2DFK" HELIX 149..156 /evidence="ECO:0000244|PDB:2DFK" HELIX 159..176 /evidence="ECO:0000244|PDB:2DFK" HELIX 182..184 /evidence="ECO:0000244|PDB:2DFK" HELIX 188..193 /evidence="ECO:0000244|PDB:2DFK" TURN 194..196 /evidence="ECO:0000244|PDB:2DFK" HELIX 197..199 /evidence="ECO:0000244|PDB:2DFK" HELIX 200..218 /evidence="ECO:0000244|PDB:2DFK" HELIX 222..234 /evidence="ECO:0000244|PDB:2DFK" HELIX 242..246 /evidence="ECO:0000244|PDB:2DFK" HELIX 248..265 /evidence="ECO:0000244|PDB:2DFK" HELIX 274..299 /evidence="ECO:0000244|PDB:2DFK" HELIX 301..310 /evidence="ECO:0000244|PDB:2DFK" STRAND 311..313 /evidence="ECO:0000244|PDB:4MT7" HELIX 319..321 /evidence="ECO:0000244|PDB:2DFK" STRAND 326..337 /evidence="ECO:0000244|PDB:2DFK" STRAND 343..350 /evidence="ECO:0000244|PDB:2DFK" STRAND 353..359 /evidence="ECO:0000244|PDB:2DFK" STRAND 367..374 /evidence="ECO:0000244|PDB:2DFK" HELIX 375..377 /evidence="ECO:0000244|PDB:2DFK" STRAND 378..382 /evidence="ECO:0000244|PDB:2DFK" STRAND 385..387 /evidence="ECO:0000244|PDB:2DFK" STRAND 389..391 /evidence="ECO:0000244|PDB:2DFK" STRAND 394..407 /evidence="ECO:0000244|PDB:2DFK" STRAND 409..413 /evidence="ECO:0000244|PDB:2DFK" HELIX 417..440 /evidence="ECO:0000244|PDB:2DFK" HELIX 446..458 /evidence="ECO:0000244|PDB:2DFK" SEQUENCE 493 AA; 58157 MW; 41040671B9398BFA CRC64; MQWIRGGSGM LITGDSIVSA EAVWDHVTMA NRGVAFKAGD VIKVLDASNK DWWWGQIDDE EGWFPASFVR LWVNQEDGVE EGPSDVQNGH LDPNSDCLCL GRPLQNRDQM RANVINEIMS TERHYIKHLK DICEGYLKQC RKRRDMFSDE QLKVIFGNIE DIYRFQMGFV RDLEKQYNND DPHLSEIGPC FLEHQDGFWI YSEYCNNHLD ACMELSKLMK DSRYQHFFEA CRLLQQMIDI AIDGFLLTPV QKICKYPLQL AELLKYTAQD HSDYRYVAAA LAVMRNVTQQ INERKRRLEN IDKIAQWQAS VLDWEGDDIL DRSSELIYTG EMAWIYQPYG RNQQRVFFLF DHQMVLCKKD LIRRDILYYK GRIDMDKYEV IDIEDGRDDD FNVSMKNAFK LHNKETEEVH LFFAKKLEEK IRWLRAFREE RKMVQEDEKI GFEISENQKR QAAMTVRKAS KQKGRVGEEE NQSLELKRAC EVLQRLWSPG KKS
Research Areas
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ARHGEF9 belongs to a family of Rho-like GTPases that act as molecular switches by cycling from the active GTP-bound state to the inactive GDP-bound state. These proteins are key regulators of the actin cytoskeleton and are involved in cell signaling.


Xiang,S., J. Mol. Biol. 359 (1), 35-46 (2006)Harvey,K., J. Neurosci. 24 (25), 5816-5826 (2004)Grosskreutz,Y., Biol. Chem. 382 (10), 1455-1462 (2001)Kins,S., Nat. Neurosci. 3 (1), 22-29 (2000)

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$ 277.78
Cat# BP2713c
Availability: 2 weeks
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