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4-Amino-3,5-dibrombenzonitril


19 390  results were found

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Artikel-Nr: (ICNA0210122805)

Lieferant:  MP Biomedicals
Hersteller-Artikelnummer:: 0210122805
Lokale Artikelnummer:: ICNA0210122805
Beschreibung:   D-Pantothenic acid is an essential vitamin (except in horses, ruminants). Pantothenic acid is involved in a number of biological reactions including: A precursor in the biosynthesis of coenzyme A, production of energy, catabolism of fatty acids and amino acids, synthesis of fatty acids, phospholipids, sphingolipids, cholesterol and steroid hormones, synthesis of heme and the neurotransmitter acetylcholine and involved in regulation of gene expression and in signal transduction.
VE:  1 * 5 g
Artikel-Nr: (BOSSBS-13736R-CY7)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13736R-CY7
Lokale Artikelnummer:: BOSSBS-13736R-CY7
Beschreibung:   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
VE:  1 * 100 µl
Lieferant:  Cytiva
Hersteller-Artikelnummer:: 25-9004-72
Lokale Artikelnummer:: GEHE25-9004-72
Beschreibung:   These versatile fluorophores can tolerate a pH range of 3 - 10 for use in a variety of applications at biologically relevant pHs. The dyes are also DMSO tolerant and photostable to enable transfer from storage to assay without loss of performance. The aqueous solubility eliminates the need for organic solvents in the assay buffers. Fluors are thoroughly QC tested to ensure high levels of chromophore and reactive dye content.
VE:  1 * 150 µG

Lieferant:  ProSci Inc.
Hersteller-Artikelnummer:: 27-172
Lokale Artikelnummer:: PRSI27-172
Beschreibung:   The GLP2 receptor (GLP2R) is a G protein-coupled receptor superfamily member closely related to the glucagon receptor ans GLP1 receptor. Glucagon-like peptide-2 (GLP2) is a 33-amino acid proglucagon-derived peptide produced by intestinal enteroendocrine cells. Like glucagon-like peptide-1 (GLP1) and glucagon itself, it is derived from the proglucagon peptide encoded by the GCG gene. GLP2 stimulates intestinal growth and upregulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. Moreover, GLP2 prevents intestinal hypoplasia resulting from total parenteral nutrition. GLP2R, a G protein-coupled receptor superfamily member is expressed in the gut and closely related to the glucagon receptor (GCGR) and the receptor for GLP1 (GLP1R). The GLP2 receptor (GLP2R) is a G protein-coupled receptor superfamily member closely related to the glucagon receptor ans GLP1 receptor. Glucagon-like peptide-2 (GLP2) is a 33-amino acid proglucagon-derived peptide produced by intestinal enteroendocrine cells. Like glucagon-like peptide-1 (GLP1) and glucagon itself, it is derived from the proglucagon peptide encoded by the GCG gene. GLP2 stimulates intestinal growth and upregulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. Moreover, GLP2 prevents intestinal hypoplasia resulting from total parenteral nutrition. GLP2R, a G protein-coupled receptor superfamily member is expressed in the gut and closely related to the glucagon receptor (GCGR) and the receptor for GLP1 (GLP1R).
VE:  1 * 50 µG
Lieferant:  Sigma-Aldrich
Beschreibung:   L(+)-Milchsäure 30% in wässriger Lösung, Sigma-Aldrich®
Lieferant:  Biosensis
Beschreibung:   The Biosensis Mouse and Rat proNGF Rapid enzyme-linked immunosorbent assay (ELISA) Kit is a sandwich ELISA that allows the quantification of rodent full-length proNGF protein in less than 4 hours in cell culture supernatants, cell lysates and tissue homogenates only if used as directed. This ELISA Kit has also successfully been used on mouse urine samples (Ryu JC et al., 2018). Please refer to the kit protocol for specific use instructions for each substrate application.

This ELISA kit contains a recombinant mouse proNGF standard expressed in E.coli and consists of a pre-coated anti-proNGF capture antibody, a biotinylated anti-proNGF detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the concentration of proNGF present in samples and protein standards. A proNGF positive control (QC sample) is provided to assure consistent assay performance. This ELISA kit detects rat proNGF due to high degree of homology (96%) with mouse proNGF based on amino acid sequence, and the ability of this kit in detecting proNGF in rat PC12 cell lysates and rat brain tissue homogenate. In the absence of a true rat proNGF standard, results may be expressed as 'mouse proNGF equivalents'. This ELISA kit shows only 20% reactivity with the human form of proNGF and is therefore not suitable to quantify human proNGF. No cross-reactivity was observed with mature mouse NGF and full-length proBDNF when tested in assay buffer.

The antibodies used in this ELISA kit bind epitopes within the pro-domain (capture) and mature domain (detection) of the protein, thus this ELISA assay does not detect the pro-domain peptide. This kit has not been tested for other applications. Sufficient amount of proNGF standard is supplied to allow for spike- and recovery experiments in order to validate this ELISA assay for other sample matrices if required.
Artikel-Nr: (BOSSBS-13736R)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13736R
Lokale Artikelnummer:: BOSSBS-13736R
Beschreibung:   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
VE:  1 * 100 µl
Artikel-Nr: (BOSSBS-13736R-CY3)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13736R-CY3
Lokale Artikelnummer:: BOSSBS-13736R-CY3
Beschreibung:   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
VE:  1 * 100 µl
Lieferant:  VACUUBRAND
Hersteller-Artikelnummer:: 20696735
Lokale Artikelnummer:: VACU20696735
Beschreibung:   Die VARIO® Chemiepumpeneinheit stellt Vakuumkontrolle durch präzise und ständige Anpassung der Motordrehzahl der Membranpumpe bereit. Die Motordrehzahlregelung auf Anforderung verlängert die Lebensdauer der Membran beträchtlich.
VE:  1 * 1 ST

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13736R-A555
Lokale Artikelnummer:: BOSSBS-13736R-A555
Beschreibung:   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
VE:  1 * 100 µl
Lieferant:  Bernd Kraft
Beschreibung:   L(+)-Milchsäure ≥90%, reinst

Lieferant:  ProSci Inc.
Hersteller-Artikelnummer:: 34-120
Lokale Artikelnummer:: PRSI34-120
Beschreibung:   Recognises a single protein of 33-34 kDa, identified as the prostate specific antigen (PSA). This mAb is highly specific to PSA and stains prostatic secretory and ductal epithelium in both normal and neoplastic tissues. PSA is a chymotrypsin-like serine protease (kallikrein family) exclusively produced by the prostate epithelium, and abundant in seminal fluid. PSA can be detected in the sera of patients with prostatic carcinoma. It is predominantly complexed to a liver-derived serine protease inhibitor, alpha-1-antichymotrypsin (ACT). A higher proportion of serum PSA is complexed to ACT in prostate cancer than in benign prostate hyperplasia.
VE:  1 * 100 µG
New Product

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13736R-A647
Lokale Artikelnummer:: BOSSBS-13736R-A647
Beschreibung:   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
VE:  1 * 100 µl
Lieferant:  MP Biomedicals
Beschreibung:   Amphotericin B is a polyene antifungal antibiotic from Streptomyces. It has an affinity for sterols, primarily ergosterols, of fungal cell membranes. It forms channels in the membranes, causing small molecules to leak out which contributes to cell death.
Artikel-Nr: (BOSSBS-13736R-CY5)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13736R-CY5
Lokale Artikelnummer:: BOSSBS-13736R-CY5
Beschreibung:   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
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13736R-HRP
Lokale Artikelnummer:: BOSSBS-13736R-HRP
Beschreibung:   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
VE:  1 * 100 µl
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Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das call noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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