You Searched For: Guanine

Catalog Number: (BOSSBS-3460R-A680)

Supplier: Bioss

Description: The protein encoded by this gene catalyses the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has been shown to be a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Two transcript variants encoding different isoforms have been found for this gene.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11459R-A350)

Supplier: Bioss

Description: FARP2 is a 1,545 amino acid protein that contains one FERM domain, one DH domain and two PH domains. It exists as two alternatively spliced isoforms that are abundantly expressed in brain, lung, and testis as well as in embryonic hippocampal and cortical neurons. FARP2 functions as a Rho-guanine nucleotide exchange factor that activates RAC1 and is thought to regulate neurite remodeling of embryonic neurons. Sema3A binding to neuropilin-1 induces the dissociation of FARP2 from plexin-A1, thereby activating FARP2's Rac GEF activity which is critical for repulsion of outgrowing axons and suppression of neuronal adhesion. Downregulation of the FARP2 gene has been implicated in autism.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3460R-FITC)

Supplier: Bioss

Description: The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has been shown to be a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13698R-A680)

Supplier: Bioss

Description: RAPGEF6 is a guanine nucleotide exchange factor (GEF) that is expressed in a variety of tissues. Localizing to the cytoplasm and translocated to the plasma membrane upon ligand binding, RAPGEF6 contains an N-terminal Ras-GEF domain, a cyclic nucleotide monophosphate-binding domain, a PDZ (PSD-95/DlgA/ZO-1) domain, a Ras-associating (RA) domain and a Ras exchanger motif. RAPGEF6 is closely related to RAPGEF2 and both proteins exhibit GEF activity specific towards Rap 1 and Rap 2. In addition, RAPGEF6 is capable of binding to M-Ras via its RA domain. Due to alternative splicing events, two additional isoforms exist for RAPGEF6, namely PDZ-GEF2A and PDZ-GEF2B.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11709R-CY3)

Supplier: Bioss

Description: Mutations in the ALS2 gene result in a number of juvenile recessive motor neuron diseases (MNDs), including juvenile primary lateral sclerosis (JPLS), a recessive form of amyotrophic lateral sclerosis (ALS2); infantile onset ascending hereditary spastic paralysis (IAHSP); and a form of complicated hereditary spastic paraplegia (cHSP). The ALS2 gene encodes the Alsin protein. Alsin acts as a guanine nucleotide exchange factor for Rab5, a modulator of the endocytic pathway. Alsin is a cytosolic protein that is associated with small, punctate membrane structures. Therefore, Alsin may mediate membrane transport events, potentially linking endocytic processes and actin cytoskeleton remodeling. The ALS2 C-terminal-like protein (ALS2CL) also modulates Rab 5 activity.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11844R-A350)

Supplier: Bioss

Description: GEFT is a 580 amino acid cytoplasmic protein that is highly expressed in excitable tissues such as brain, heart and muscle, and weakly expressed in small intestine, colon, liver, placenta and lung. GEFT may play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. GEFT works as a guanine nucleotide exchange factor for the Rho family of small GTPases and links specifically to G alpha q/11-coupled receptors in Rho A activation. GEFT is an important regulator of processes involved in axon and dendrite formation. Involved in skeletal myogenesis, GEFT seems to be an exchange factor primarily for Rac 1 in neurons. Existing as two alternatively spliced variants, GEFT contains a DH (DBL-homology) domain and a PH domain.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11844R-A647)

Supplier: Bioss

Description: GEFT is a 580 amino acid cytoplasmic protein that is highly expressed in excitable tissues such as brain, heart and muscle, and weakly expressed in small intestine, colon, liver, placenta and lung. GEFT may play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. GEFT works as a guanine nucleotide exchange factor for the Rho family of small GTPases and links specifically to G alpha q/11-coupled receptors in Rho A activation. GEFT is an important regulator of processes involved in axon and dendrite formation. Involved in skeletal myogenesis, GEFT seems to be an exchange factor primarily for Rac 1 in neurons. Existing as two alternatively spliced variants, GEFT contains a DH (DBL-homology) domain and a PH domain.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11458R-A350)

Supplier: Bioss

Description: EPHEXIN is a 710 amino acid protein that localizes to both the membrane and the cytoplasm and contains one SH3 domain, one PH domain and one DH domain. Expressed at high levels in brain and present at lower levels in lung tissue, EPHEXIN interacts with EphA4 and functions as a guanine nucleotide exchange factor (GEF) that is capable of activating Rho A, Rac 1 and Cdc42 and is thought to play a role in axon guidance and growth cone collapse. EPHEXIN is subject to Src-dependent phosphorylation, an event that increases the GEF activity of EPHEXIN toward Rho A. Human EPHEXIN, which exists as multiple alternatively spliced isoforms, shares a high degree of sequence homology with its mouse counterpart, suggesting a conserved role between species.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1961R-A488)

Supplier: Bioss

Description: May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12432R-CY3)

Supplier: Bioss

Description: DOCK 4 is a cytoplasmic peripheral membrane protein that belongs to the DOCK family of cytokinesis-regulating proteins. Expressed ubiquitously with highest expression in prostate, ovary and skeletal muscle, DOCK 4 functions as a guanine nucleotide exchange factor (GEF) that activates the small GTPase Rap 1 and, via this activation, plays a role in the regulation of adherens junctions between cells. Similar to other DOCK family members, DOCK 4 contains an N-terminal SH3 domain, a C-terminal proline-rich region and two internal DOCK homology regions designated DHR1 and DHR2. Defects in the gene encoding DOCK 4 result in the inactivation of Rap 1 and are, thus, implicated in the pathogenesis of various cancers such as ovarian, prostate, glioma and colorectal carcinomas. Four isoforms of DOCK 4 are expressed due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12523R-CY5)

Supplier: Bioss

Description: ADP-ribosylation factors (ARFs) are highly conserved guanine nucleotide-binding proteins that enhance the ADP-ribosyltransferase activity of cholera toxin. ARF抯 are important in eukaryotic vesicular trafficking pathways and activating phospholipase D. ARL4 (ADP-ribosylation factor-like protein 4A) is a member of the ARF-like protein (ARL) subfamily of small GTPases. It contains a C terminal nuclear localization signal (NLS) region that interacts with Importin-? ARL4 localizes to the nucleus and is found in a variety of tissues, but is predominantly expressed in spermatogonia and Sertoli cells. It is most closely related to ARL6 and ARL7. Unlike ARFs, ARL4 does not activate the cholera toxin ADP-ribosyltranferase. ARL4 may play a role in neurogenesis during embryonic development and somitogenesis in the early stages of adult spermatogenesis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3382R-A647)

Supplier: Bioss

Description: The protein encoded by this gene is a guanine nucleotide exchange factor (GEF) similar to the Saccharomyces cerevisiae CDC25 gene product. Functional analysis has demonstrated that this protein stimulates the dissociation of GDP from RAS protein. The studies of the similar gene in mouse suggested that the Ras-GEF activity of this protein in brain can be activated by Ca2+ influx, muscarinic receptors, and G protein beta-gamma subunit. Mouse studies also indicated that the Ras-GEF signaling pathway mediated by this protein may be important for long-term memory. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Mar 2009]

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13698R-CY7)

Supplier: Bioss

Description: RAPGEF6 is a guanine nucleotide exchange factor (GEF) that is expressed in a variety of tissues. Localizing to the cytoplasm and translocated to the plasma membrane upon ligand binding, RAPGEF6 contains an N-terminal Ras-GEF domain, a cyclic nucleotide monophosphate-binding domain, a PDZ (PSD-95/DlgA/ZO-1) domain, a Ras-associating (RA) domain and a Ras exchanger motif. RAPGEF6 is closely related to RAPGEF2 and both proteins exhibit GEF activity specific towards Rap 1 and Rap 2. In addition, RAPGEF6 is capable of binding to M-Ras via its RA domain. Due to alternative splicing events, two additional isoforms exist for RAPGEF6, namely PDZ-GEF2A and PDZ-GEF2B.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-10271R-A350)

Supplier: Bioss

Description: The Vav family of Rho guanine nucleotide exchange factors (GEFs) orchestrate signaling events following lymphocyte antigen receptor activation. Vav3, like Vav (also known as Vav1 or p95Vav), undergoes tyrosine phosphorylation downstream of T cell receptor cross-linkage, and subsequently interacts with 2 adaptor molecules, SLP76 and 3BP2. Following these events, however, the paths of Vav and Vav3 diverge; Vav affects IL-2 promotor activity, while Vav3 impacts gene transcription linked to serum response element (SRE). Furthermore, Vav3 expression follows a cell cycle-dependent pattern, with transient upregulation occuring during mitosis. Encforced Vav3 expression leads to the appearance of multinucleate cells, implicating a role for Vav3 in the control of cytokinesis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12432R-A350)

Supplier: Bioss

Description: DOCK 4 is a cytoplasmic peripheral membrane protein that belongs to the DOCK family of cytokinesis-regulating proteins. Expressed ubiquitously with highest expression in prostate, ovary and skeletal muscle, DOCK 4 functions as a guanine nucleotide exchange factor (GEF) that activates the small GTPase Rap 1 and, via this activation, plays a role in the regulation of adherens junctions between cells. Similar to other DOCK family members, DOCK 4 contains an N-terminal SH3 domain, a C-terminal proline-rich region and two internal DOCK homology regions designated DHR1 and DHR2. Defects in the gene encoding DOCK 4 result in the inactivation of Rap 1 and are, thus, implicated in the pathogenesis of various cancers such as ovarian, prostate, glioma and colorectal carcinomas. Four isoforms of DOCK 4 are expressed due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12432R-FITC)

Supplier: Bioss

Description: DOCK 4 is a cytoplasmic peripheral membrane protein that belongs to the DOCK family of cytokinesis-regulating proteins. Expressed ubiquitously with highest expression in prostate, ovary and skeletal muscle, DOCK 4 functions as a guanine nucleotide exchange factor (GEF) that activates the small GTPase Rap 1 and, via this activation, plays a role in the regulation of adherens junctions between cells. Similar to other DOCK family members, DOCK 4 contains an N-terminal SH3 domain, a C-terminal proline-rich region and two internal DOCK homology regions designated DHR1 and DHR2. Defects in the gene encoding DOCK 4 result in the inactivation of Rap 1 and are, thus, implicated in the pathogenesis of various cancers such as ovarian, prostate, glioma and colorectal carcinomas. Four isoforms of DOCK 4 are expressed due to alternative splicing events.

UOM: 1 * 100 µl