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Mass+Spectrometry
Numéro de catalogue:
(BOSSBS-13736R)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13736R-CY3)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13736R-A647)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BSENR-1697-100)
Fournisseur:
Biosensis
Description:
The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).
UOM:
1 * 100 µl
Fournisseur:
Agilent
Description:
Features and benefits for the low thermal mass column modules, or the LTM II.
Numéro de catalogue:
(BOSSBS-13736R-A555)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BSENC-1698-100)
Fournisseur:
Biosensis
Description:
The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13736R-A350)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13736R-A680)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13736R-A750)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Fournisseur:
NEUBERT VOLUM. GLASSWAERE
Description:
Borosilicate glass 3,3.
Fournisseur:
Restek
Description:
This GC-MS cleaning kit has assembled all of the necessary components for cleaning and polishing your ion source.
Fournisseur:
SGE a Trajan company
Description:
Construite pour optimiser la sensibilité de votre analyse en masse.
Numéro de catalogue:
(PIER90115)
Fournisseur:
Thermo Fisher Scientific
Description:
Thermo Scientific 50% Hydroxylamine is a 10X quenching reagent for amine-reactive isobaric mass tag labeling experiments.
UOM:
1 * 5 mL
Fournisseur:
Thermo Fisher Scientific
Description:
The SilTite µ-Union is a connector for GC capillary columns, giving zero dead volume. It has low thermal mass, is only 9 mm in length and has a mass <0,5 g.
Fournisseur:
Industrial Physics
Description:
Magnet probes to measure object temperature, fitted with an ultra strong magnet, but still with a very low mass and size.
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