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2,5-Dimethoxy-6-fluorophenylboronic+acid
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2,5-Dimethoxy-6-fluorophenylboronic+acid
Catalog Number:
(10290-564)
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.
Catalog Number:
(10290-568)
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.
Catalog Number:
(10257-182)
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.
Catalog Number:
(76084-768)
Supplier:
Bioss
Description:
P73 protein is a structural and functional homologue of p53, a tumor suppressor gene. In this study, The p73 protein, p19ras, by the yeast two-hybrid screening method. Alternative splicing of the proto-oncogene H-ras pre-mRNA has led to two distinct transcripts, Ras proteins are known to be small membrane-localized guanine nucleotide-binding proteins. However, unlike other Ras proteins, p19ras is localized in the nucleus and the cytosol and its interaction with P73 protein occurred exclusively in the nucleus. Oncogenic MDM2 (mouse double minutes 2) is a known repressor of p73 transcriptional activity. In this study, when p19ras was bound to MDM2, it further inhibited the association of MDM2 to the p73 protein. Therefore, this study presents a novel pathway of Ras signaling that occurs in the nucleus, involving p19ras and p73.
Catalog Number:
(10257-152)
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.
Catalog Number:
(10259-856)
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.
Catalog Number:
(10255-992)
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.
Catalog Number:
(10280-138)
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.
Catalog Number:
(77440-518)
Supplier:
Bioss
Description:
The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins. ARFs influence vesicle trafficking and signal transduction in eukaryotic cells. ARF6 plays a role in protein trafficking near the plasma membrane, including receptor recycling, cell adhesion and cell migration. ARF6 colocalizes with the ARF guanine nucleotide-exchange protein (GEP) BRAG2, also designated GEP100. BRAG2 is ubiquitously expressed as two isoforms, BRAG2a and BRAG2b, which can cycle between the cytoplasm and the nucleus. BRAG2, via its interaction with ARF6, is involved in the regulation of cell adhesion by controlling Integrin 1 endocytosis and E-cadherin redistribution. BRAG2 has also been shown to bind directly to Tyr1068/1086-phosphorylated EGFR to activate ARF6, which induces tumor invasion in MCF7 cells. Therefore, BRAG2 may contribute to the metastasis and malignancy of some breast cancer cells.
Catalog Number:
(10257-178)
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.
Catalog Number:
(76011-688)
Supplier:
Prosci
Description:
The protein encoded by this gene is a member of the PSCD family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of PSCDs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. The encoded protein exhibits GEP activity in vitro with ARF1, ARF3, and ARF6 and is 83% homologous to CYTH1. Two transcript variants encoding different isoforms have been found for this gene.
Catalog Number:
(10333-942)
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.
Catalog Number:
(10333-932)
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.
Catalog Number:
(10259-854)
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.
Catalog Number:
(10280-148)
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.
Catalog Number:
(10261-166)
Supplier:
Bioss
Description:
MOCA (modifier of cell adhesion), also known as Presenilin-binding protein (PBP) or dedicator of cytokinesis protein 3 (DOCK3), is a 2030 amino acid cytoplasmic protein belonging to the DOCK family. MOCA interacts with Presenilin proteins and has the ability to stimulate Tau phosphorylation suggesting that MOCA may be involved in Alzheimer disease. MOCA is also thought to be a guanine nucleotide exchange factor (GEF) which activates small GTPases by exchanging bound GDP for free GTP. Analysis of ectopic expression suggests that MOCA may affect the function of small GTPases involved in the regulation of Actin cytoskeleton or cell adhesion receptors. MOCA is localized to the neuropil, and sometimes in pyramidal cells, in normal brains, while in Alzheimer disease brains, MOCA is present in neurofibrillary tangles.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
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