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Catalog Number: (BOSSBS-13274R-A647)
Supplier: Bioss
Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13274R-CY7)
Supplier: Bioss
Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0597R-A488)
Supplier: Bioss
Description: SCRG1 (scrapie-responsive protein 1) is a 98 amino acid secreted protein that belongs to the SCRG1 family. The SCRG1 protein contains a 20-amino acid signal peptide, and is expressed abundantly in the central nervous system of human adult, but not at all in fetal brain. The protein is targeted to the Golgi apparatus and large dense-core vesicles/secretory granules in neurons. High levels of SCRG1 transcripts are also observed in testis and aorta. SCRG1 is associated with neurodegenerative changes observed in transmissible spongiform encephalopathies. It may play a role in host response to prion-associated infections. The SCRG1 protein may be partly included in the membrane or secreted by the cells due to its hydrophobic N-terminus. The human and mouse SCRG1 proteins share 83% sequence identity. The SCRG1 gene is conserved in chimpanzee, cow, mouse, rat and chicken, and maps to human chromosome 4q34.1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0597R-HRP)
Supplier: Bioss
Description: SCRG1 (scrapie-responsive protein 1) is a 98 amino acid secreted protein that belongs to the SCRG1 family. The SCRG1 protein contains a 20-amino acid signal peptide, and is expressed abundantly in the central nervous system of human adult, but not at all in fetal brain. The protein is targeted to the Golgi apparatus and large dense-core vesicles/secretory granules in neurons. High levels of SCRG1 transcripts are also observed in testis and aorta. SCRG1 is associated with neurodegenerative changes observed in transmissible spongiform encephalopathies. It may play a role in host response to prion-associated infections. The SCRG1 protein may be partly included in the membrane or secreted by the cells due to its hydrophobic N-terminus. The human and mouse SCRG1 proteins share 83% sequence identity. The SCRG1 gene is conserved in chimpanzee, cow, mouse, rat and chicken, and maps to human chromosome 4q34.1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11910R-A647)
Supplier: Bioss
Description: ACBD3 (acyl-CoA-binding domain-containing protein 3), also known as GCP60 (Golgi resident protein GCP60), GOCAP1, PAP7 or GOLPH1, is a Golgi apparatus membrane protein that contains one ACB (acyl-CoA-binding) domain and one GOLD (Golgi dynamics) domain which is essential for its interaction with other proteins. Expressed ubiquitously with highest expression in ovary and testis, ACBD3 is responsible for maintaining Golgi structure and, through binding to Giantin (golgin subfamily B member 1), functions to mediate protein transport between the Golgi and the endoplasmic reticulum (ER). Changes in the subcellular location of ACBD3 trigger signaling cascades within the Golgi that regulate cell fate and cell cycle progression. Additionally, ACBD3 is thought to act as a peripheral-type benzodiazepine receptor-associated protein, possibly playing a role in hormonal regulation and steroid formation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11910R-A350)
Supplier: Bioss
Description: ACBD3 (acyl-CoA-binding domain-containing protein 3), also known as GCP60 (Golgi resident protein GCP60), GOCAP1, PAP7 or GOLPH1, is a Golgi apparatus membrane protein that contains one ACB (acyl-CoA-binding) domain and one GOLD (Golgi dynamics) domain which is essential for its interaction with other proteins. Expressed ubiquitously with highest expression in ovary and testis, ACBD3 is responsible for maintaining Golgi structure and, through binding to Giantin (golgin subfamily B member 1), functions to mediate protein transport between the Golgi and the endoplasmic reticulum (ER). Changes in the subcellular location of ACBD3 trigger signaling cascades within the Golgi that regulate cell fate and cell cycle progression. Additionally, ACBD3 is thought to act as a peripheral-type benzodiazepine receptor-associated protein, possibly playing a role in hormonal regulation and steroid formation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11910R-CY3)
Supplier: Bioss
Description: ACBD3 (acyl-CoA-binding domain-containing protein 3), also known as GCP60 (Golgi resident protein GCP60), GOCAP1, PAP7 or GOLPH1, is a Golgi apparatus membrane protein that contains one ACB (acyl-CoA-binding) domain and one GOLD (Golgi dynamics) domain which is essential for its interaction with other proteins. Expressed ubiquitously with highest expression in ovary and testis, ACBD3 is responsible for maintaining Golgi structure and, through binding to Giantin (golgin subfamily B member 1), functions to mediate protein transport between the Golgi and the endoplasmic reticulum (ER). Changes in the subcellular location of ACBD3 trigger signaling cascades within the Golgi that regulate cell fate and cell cycle progression. Additionally, ACBD3 is thought to act as a peripheral-type benzodiazepine receptor-associated protein, possibly playing a role in hormonal regulation and steroid formation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11910R-A680)
Supplier: Bioss
Description: ACBD3 (acyl-CoA-binding domain-containing protein 3), also known as GCP60 (Golgi resident protein GCP60), GOCAP1, PAP7 or GOLPH1, is a Golgi apparatus membrane protein that contains one ACB (acyl-CoA-binding) domain and one GOLD (Golgi dynamics) domain which is essential for its interaction with other proteins. Expressed ubiquitously with highest expression in ovary and testis, ACBD3 is responsible for maintaining Golgi structure and, through binding to Giantin (golgin subfamily B member 1), functions to mediate protein transport between the Golgi and the endoplasmic reticulum (ER). Changes in the subcellular location of ACBD3 trigger Signalling cascades within the Golgi that regulate cell fate and cell cycle progression. Additionally, ACBD3 is thought to act as a peripheral-type benzodiazepine receptor-associated protein, possibly playing a role in hormonal regulation and steroid formation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12514R-A750)
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 and they play a central role in the maintenance of organelle integrity, assembly of coat proteins and activation of phospholipase D (PC-PLD). ARFRP1 (ADP-ribosylation factor related protein 1), also known as ARP or ARL18, is a 201 amino acid membrane-associated GTPase that localizes to the plasma membrane and the Golgi apparatus and is related to the ARF family of regulatory proteins. Expressed in a variety of tissues, ARFRP1 interacts with SYS1 and is thought to be involved in plasma membrane-related Signalling events. ARFRP1 exists as multiple alternatively spliced isoforms and is encoded by a gene which maps to a gene cluster on chromosome 20 that is commonly overexpressed in tumours, suggesting a role for ARFRP1 in carcinogenesis.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12514R-HRP)
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 and they play a central role in the maintenance of organelle integrity, assembly of coat proteins and activation of phospholipase D (PC-PLD). ARFRP1 (ADP-ribosylation factor related protein 1), also known as ARP or ARL18, is a 201 amino acid membrane-associated GTPase that localizes to the plasma membrane and the Golgi apparatus and is related to the ARF family of regulatory proteins. Expressed in a variety of tissues, ARFRP1 interacts with SYS1 and is thought to be involved in plasma membrane-related signaling events. ARFRP1 exists as multiple alternatively spliced isoforms and is encoded by a gene which maps to a gene cluster on chromosome 20 that is commonly overexpressed in tumors, suggesting a role for ARFRP1 in carcinogenesis.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1071R)
Supplier: Bioss
Description: This gene belongs to the Ras oncogene family, whose members are related to the transforming genes of mammalian sarcoma retroviruses. The products encoded by these genes function in signal transduction pathways. These proteins can bind GTP and GDP, and they have intrinsic GTPase activity. This protein undergoes a continuous cycle of de- and re-palmitoylation, which regulates its rapid exchange between the plasma membrane and the Golgi apparatus. Mutations in this gene cause Costello syndrome, a disease characterized by increased growth at the prenatal stage, growth deficiency at the postnatal stage, predisposition to tumor formation, mental retardation, skin and musculoskeletal abnormalities, distinctive facial appearance and cardiovascular abnormalities. Defects in this gene are implicated in a variety of cancers, including bladder cancer, follicular thyroid cancer, and oral squamous cell carcinoma. Multiple transcript variants, which encode different isoforms, have been identified for this gene. [provided by RefSeq].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9728R-A680)
Supplier: Bioss
Description: Beta-1,4-galactosyltransferases (beta-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a beta-1,4 linkage to an acceptor sugar. There are seven members of the beta-1,4-Gal-T family, all of which are directed to the golgi apparatus through a hydrophobic sequence at the N-terminus. Beta-1,4-Gal-T7, also known as B4GALT7 or XGALT1, is a 327 amino acid single-pass type II membrane protein that is expressed at high levels in heart, pancreas and liver. Beta-1,4-Gal-T7 uses manganese to catalyse the UDP-dependent biosynthesis of glycosphingolipids. The gene encoding beta-1,4-Gal-T7 is mutated in Ehlers-Danlos syndrome progeroid type (EDSP), a variant form of Ehlers-Danlos syndrome characterised by progeroid facies, mild mental retardation, short stature, skin hyperextensibility, moderate skin fragility, joint hypermobility principally in digits. Beta-1,4-galactosyltransferases (Beta-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a beta-1,4 linkage to an acceptor sugar.
UOM: 1 * 100 µl


Catalog Number: (USBI133757)
Supplier: US Biological
Description: Anti-SPDL1 Mouse Monoclonal Antibody [clone: 2F4]
UOM: 1 * 100 µG


Catalog Number: (BOSSBS-13492R-CY3)
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


Catalog Number: (BOSSBS-13492R-A750)
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


Catalog Number: (BOSSBS-13492R-A680)
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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