You Searched For: Palmitoyl+chloride

Catalog Number: (BOSSBS-13492R-A350)

Supplier: Bioss

Description: The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).

UOM: 1 * 100 µl

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Catalog Number: (PRSI30-222)

Supplier: ProSci Inc.

Description: Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It converts L-serine and palmitoyl-CoA to 3-oxosphinganine with pyridoxal 5'-phosphate as a cofactor. SPTLC1 is the long chain base subunit 1 of serine palmitoyltransferase. Mutations in SPTLC1 gene were identified in patients with hereditary sensory neuropathy type 1.Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It converts L-serine and palmitoyl-CoA to 3-oxosphinganine with pyridoxal 5'-phosphate as a cofactor. The product of this gene is the long chain base subunit 1 of serine palmitoyltransferase. Mutations in this gene were identified in patients with hereditary sensory neuropathy type 1. Alternatively spliced variants encoding different isoforms have been identified.

UOM: 1 * 50 µG

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Catalog Number: (USBI042277-BIOTIN)

Supplier: US Biological

Description: Anti-SPTLC2 Rabbit Polyclonal Antibody (Biotin)

UOM: 1 * 200 µl

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Catalog Number: (BOSSBS-12944R-FITC)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-FITC)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-HRP)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13492R-A647)

Supplier: Bioss

Description: The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).

UOM: 1 * 100 µl

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Catalog Number: (PRSI25-328)

Supplier: ProSci Inc.

Description: LASS5 may be either a bona fide (dihydro)ceramide synthase or a modulator of its activity. When it is overexpressed in cells it is involved in the production of sphingolipids containing mainly only one fatty acid donor (N-linked palmitoyl- (C16) ceramide) in a fumonisin B1-independent manner.

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-7112R-CY5.5)

Supplier: Bioss

Description: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis (By similarity). Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7112R-A488)

Supplier: Bioss

Description: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis (By similarity). Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.

UOM: 1 * 100 µl

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Catalog Number: (BSENC-1649-100)

Supplier: Biosensis

Description: GAP43 is very abundant protein which is found concentrated in neurons. One group discovered it as one of three proteins which becomes unregulated during the regeneration of the toad optic nerve (1). Three GAPs (Growth associated proteins) were discovered, and the number 43 comes from the apparent SDS-PAGE molecular weight of the one named GAP43. The HGNC name for this protein is, not surprisingly, GAP43. Later work showed that GAP43 does not run on SDS-PAGE in a fashion which accurately reflects its molecular weight, and that GAP43 proteins from different species may run at different apparent molecular weights. Partly due to these features GAP43 were independently discovered by several different groups and therefore has several alternate names, such as protein F1, pp46, neuromodulin, neural phosphoprotein B-50 and calmodulin-binding protein P-57. In each case the number reflects the apparent SDS-PAGE molecular weight, and underlines the unusual properties of this molecule. Mammalian GAP43 proteins contains only 226-243 amino acids, and so the real molecular weight is 23.61-25.14 kDa. GAP43 has been extensively studied and is known to be a major protein kinase C substrate and to bind calmodulin avidly. GAP43 is anchored to the plasma membrane by palmitoylation modifications.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-A647)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (PRSI26-333)

Supplier: ProSci Inc.

Description: SPTLC2 is a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I.This gene encodes a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I. Alternatively spliced variants encoding different isoforms have been identified.

UOM: 1 * 50 µG

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Catalog Number: (PRSI4697)

Supplier: ProSci Inc.

Description: LASS5 Antibody: The LASS (longevity assurance homolog) family members represent a subgroup of the homeobox gene family and are highly conserved from yeasts to mammals. Six members of this family of proteins have been characterized (LASS1-6) and all are involved in ceramide synthesis during cell growth regulation and cancer differentiation. LASS5, also called Trh4, is a 392 amino acid endoplasmic reticulum, multi-pass membrane protein. Functioning as a dihydro-ceramide synthase, LASS5 is involved in the production of sphingolipids containing mainly one fatty acid donor (N-linked palmitoyl-ceramide) in a fumonisin B1-independent manner. It uses palmitoyl-CoA as an acyl donor and is involved in the synthesis of C14, C16 and C18-ceramide. LASS5 is the most abundantly expressed and predominant ceramide synthase isoform in lung epithelia. Recent studies show that LASS5 partially correct growth and apoptosis.

UOM: 1 * 100 µG

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Catalog Number: (USBI031558)

Supplier: US Biological

Description: Anti-ACSL1 Rabbit Polyclonal Antibody

UOM: 1 * 200 µl

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Catalog Number: (PRSI92-096)

Supplier: ProSci Inc.

Description: Acyl-Protein Thioesterase 2 is a cytoplasmic protein that belongs to the AB Hydrolase 2 family. LYPLA2 is a lysophospholipase and hydrolyses fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. LYPLA2 has hydrolase activity that converts Palmitoyl-protein to palmitate and protein. LYPLA2 regulates the multifunctional lysophospholipids by acting on biological membranes. LYPLA2 participates in Glycerophospholipid metabolism pathway, fatty acid metabolic process and lipid metabolic process.

UOM: 1 * 50 µG

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