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trans-2-Nitrocinnamic+acid
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trans-2-Nitrocinnamic+acid
Catalog Number:
(10296-492)
Supplier:
Bioss
Description:
The GGA family of proteins (Golgi-localized, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin (1?). Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) (1,2,4). GGAs have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (?adaptin ear) domain (5). The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences (3). GGA1 and GGA2 do not associate with each other, but they do colocalize on perinuclear membranes (2). The cytosolic domain of memapsin 2, but not that of memapsin 1, binds the VHS domains of GGA1 and GGA2 (6). The human GGA1 gene maps to chromosome 22 and encodes a protein that shares 45% sequence identity with GGA2 and GGA3 (1).
Catalog Number:
(10296-494)
Supplier:
Bioss
Description:
The GGA family of proteins (Golgi-localized, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin (1?). Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) (1,2,4). GGAs have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (?adaptin ear) domain (5). The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences (3). GGA1 and GGA2 do not associate with each other, but they do colocalize on perinuclear membranes (2). The cytosolic domain of memapsin 2, but not that of memapsin 1, binds the VHS domains of GGA1 and GGA2 (6). The human GGA1 gene maps to chromosome 22 and encodes a protein that shares 45% sequence identity with GGA2 and GGA3 (1).
Catalog Number:
(10296-644)
Supplier:
Bioss
Description:
The GGA family of proteins (Golgi-localized, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin (1?). Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) (1,2,4). GGAs have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (?adaptin ear) domain (5). The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences (3). GGA1 and GGA2 do not associate with each other, but they do colocalize on perinuclear membranes (2). The cytosolic domain of memapsin 2, but not that of memapsin 1, binds the VHS domains of GGA1 and GGA2 (6). The human GGA1 gene maps to chromosome 22 and encodes a protein that shares 45% sequence identity with GGA2 and GGA3 (1).
Catalog Number:
(76009-510)
Supplier:
Prosci
Description:
NCALD encodes a member of the neuronal calcium sensor (NCS) family of calcium-binding proteins. The protein contains an N-terminal myristoylation signal and four EF-hand calcium binding loops. The protein is cytosolic at resting calcium levels; however, elevated intracellular calcium levels induce a conformational change that exposes the myristoyl group, resulting in protein association with membranes and partial co-localization with the perinuclear trans-golgi network. The protein is thought to be a regulator of G protein-coupled receptor signal transduction. Several alternatively spliced variants of this gene have been determined, all of which encode the same protein; additional variants may exist but their biological validity has not been determined.
Catalog Number:
(10296-490)
Supplier:
Bioss
Description:
The GGA family of proteins (Golgi-localized, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin (1?). Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) (1,2,4). GGAs have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (?adaptin ear) domain (5). The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences (3). GGA1 and GGA2 do not associate with each other, but they do colocalize on perinuclear membranes (2). The cytosolic domain of memapsin 2, but not that of memapsin 1, binds the VHS domains of GGA1 and GGA2 (6). The human GGA1 gene maps to chromosome 22 and encodes a protein that shares 45% sequence identity with GGA2 and GGA3 (1).
Catalog Number:
(10296-482)
Supplier:
Bioss
Description:
The GGA family of proteins (Golgi-localized, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin (1?). Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) (1,2,4). GGAs have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (?adaptin ear) domain (5). The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences (3). GGA1 and GGA2 do not associate with each other, but they do colocalize on perinuclear membranes (2). The cytosolic domain of memapsin 2, but not that of memapsin 1, binds the VHS domains of GGA1 and GGA2 (6). The human GGA1 gene maps to chromosome 22 and encodes a protein that shares 45% sequence identity with GGA2 and GGA3 (1).
Catalog Number:
(10750-688)
Supplier:
Prosci
Description:
GOLPH3 Antibody: GOLPH3 was initially identified as a peripheral membrane protein localized to the trans-Golgi network, but others reported it to be primarily a mitochondrial protein that regulated the mitochondrial mass through the regulation of the mitochondria-specific phospholipid cardiolipin. GOLPH3 has since been implicated in the target of rapamycin (TOR) signalling pathway. Its overexpression in transfected cells led to and increase in anchorage-independent growth and cell proliferation in vitro. Furthermore, GOLPH3-transfected cells enhanced S6 Kinase activity in response to growth factor stimulation by EGF. Simultaneously, AKT phosphorylation increased in these cells, while these events were abrogated in GOLPH3 siRNA treated cells compared to control cells, indicating the GOLPH3 can enhance signalling through TOR-associated complexes. These results suggest that GOLPH3 is a bona fide oncogene and may be a useful target for therapeutic strategies.
Catalog Number:
(10078-984)
Supplier:
Prosci
Description:
Notch is synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase (S1 cleavage) in the trans-golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved (S2 cleavage) by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin-dependent gamma-secretase (S3 cleavage) to release the intracellular domain (NICD) from the membrane. Notch functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBP-J kappa and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs.
Supplier:
Biotium
Description:
This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.
Supplier:
Biotium
Description:
This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.
Catalog Number:
(75926-912)
Supplier:
Biotium
Description:
This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.
Catalog Number:
(76193-996)
Supplier:
Prosci
Description:
This mAb recognizes a protein of 134kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This mAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This mAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.
Catalog Number:
(75928-166)
Supplier:
Rockland Immunochemical
Description:
GOLPH3 was initially identified as a peripheral membrane protein localized to the trans-Golgi network, but others reported it to be primarily a mitochondrial protein that regulated the mitochondrial mass through the regulation of the mitochondria-specific phospholipid cardiolipin. GOLPH3 has since been implicated in the target of rapamycin (TOR) signalling pathway. Its overexpression in transfected cells led to and increase in anchorage-independent growth and cell proliferation in vitro. Furthermore, GOLPH3-transfected cells enhanced S6 Kinase activity in response to growth factor stimulation by EGF. Simultaneously, AKT phosphorylation increased in these cells, while these events were abrogated in GOLPH3 siRNA treated cells compared to control cells, indicating the GOLPH3 can enhance signalling through TOR-associated complexes. These results suggest that GOLPH3 is a bona fide oncogene and may be a useful target for therapeutic strategies.
Catalog Number:
(76012-522)
Supplier:
Prosci
Description:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Catalog Number:
(10081-740)
Supplier:
Proteintech
Description:
Cadherins are a family of transmembrane glycoproteins that mediate calcium-dependent cell-cell adhesion and play an important role in the maintenance of normal tissue architecture. E-cadherin (epithelial cadherin), also known as CDH1 (cadherin 1) or CAM 120/80, is a classical member of the cadherin superfamily which also include N-, P-, R-, and B-cadherins. It has been regarded as a marker for spermatogonial stem cells in mice. E-cadherin is expressed on the cell surface in most epithelial tissues. The extracellular region of E-cadherin establishes calcium-dependent homophilic trans binding, providing specific interaction with adjacent cells, while the cytoplasmic domain is connected to the actin cytoskeleton through the interaction with p120-, α-, β-, and γ-catenin (plakoglobin). E-cadherin is important in the maintenance of the epithelial integrity, and is involved in mechanisms regulating proliferation, differentiation, and survival of epithelial cell. E-cadherin may also play a role in tumorigenesis. It is considered to be an invasion suppressor protein and its loss is an indicator of high tumor aggressiveness. E-cadherin is sensitive to trypsin digestion in the absence of Ca2+. This polyclonal antibody recognizes 120-kDa intact E-cadherin and its 80-kDa trypsin-cleaved fragment.
Supplier:
Biotium
Description:
This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®647 is a far-red fluorescent dye (Ex/Em 650/665 nm) with excellent brightness. It also is compatible with super-resolution imaging by STORM.
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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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