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Search results for: Mouse Anti-Human GAPDH Antibodies

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#25888749   2015/03/08 To Up

Characterization and possible function of glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS in mammalian sperm.

Sperm proteins are important for the sperm cell function in fertilization. Some of them are involved in the binding of sperm to the egg. We characterized the acrosomal sperm protein detected by a monoclonal antibody (MoAb) (Hs-8) that was prepared in our laboratory by immunization of BALB/c mice with human ejaculated sperms and we tested the possible role of this protein in the binding assay.
Hasmik Margaryan, Andriy Dorosh, Jana Capkova, Pavla Manaskova-Postlerova, Anatoly Philimonenko, Pavel Hozak, Jana Peknicova

2130 related Products with: Characterization and possible function of glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS in mammalian sperm.

1mg1 Set1 Set1 Set1 Set1 Set2ug0.1 mg100ug Lyophilized1001 Set1 Set

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#25650727   2015/01/23 To Up

Detection of exosomal biomarker by electric field-induced release and measurement (EFIRM).

Exosomes are microvesicular structures that play a mediating role in intercellular communication. It is of interest to study the internal cargo of exosomes to determine if they carry disease discriminatory biomarkers. For performing exosomal analysis, it is necessary to develop a method for extracting and analyzing exosomes from target biofluids without damaging the internal content. Electric field-induced release and measurement (EFIRM) is a method for specifically extracting exosomes from biofluids, unloading their cargo, and testing their internal RNA/protein content. Using an anti-human CD63 specific antibody magnetic microparticle, exosomes are first precipitated from biofluids. Following extraction, low-voltage electric cyclic square waves (CSW) are applied to disrupt the vesicular membrane and cause cargo unloading. The content of the exosome is hybridized to DNA primers or antibodies immobilized on an electrode surface for quantification of molecular content. The EFIRM method is advantageous for extraction of exosomes and unloading cargo for analysis without lysis buffer. This method is capable of performing specific detection of both RNA and protein biomarker targets in the exosome. EFIRM extracts exosomes specifically based on their surface markers as opposed to size-based techniques. Transmission electron microscopy (TEM) and assay demonstrate the functionality of the method for exosome capture and analysis. The EFIRM method was applied to exosomal analysis of 9 mice injected with human lung cancer H640 cells (a cell line transfected to express the exosome marker human CD63-GFP) in order to test their exosome profile against 11 mice receiving saline controls. Elevated levels of exosomal biomarkers (reference gene GAPDH and protein surface marker human CD63-GFP) were found for the H640 injected mice in both serum and saliva samples. Furthermore, saliva and serum samples were demonstrated to have linearity (R = 0.79). These results are suggestive for the viability of salivary exosome biomarkers for detection of distal diseases.
Michael Tu, Fang Wei, Jieping Yang, David Wong

2254 related Products with: Detection of exosomal biomarker by electric field-induced release and measurement (EFIRM).

96 tests250tests16 Arrays/Slide10 mg96 wells2x96 well plates16 Arrays/Slide100 mg

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#23983427   // To Up

Human platelets inhibit liver fibrosis in severe combined immunodeficiency mice.

To investigate the role of human platelets in liver fibrosis.
Kazuhiro Takahashi, Soichiro Murata, Kiyoshi Fukunaga, Nobuhiro Ohkohchi

1705 related Products with: Human platelets inhibit liver fibrosis in severe combined immunodeficiency mice.

1 mg5 mg100μg100μg2.5 mg96T25mg50ug100μg0.1 ml100 50ug

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#16649249   // To Up

Cross reactivity between many anti-human antibodies for their hamster homologs provide the tools to study the signal transduction pathway activated by asbestos and SV40 in the malignant mesothelioma model.

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Barbara Kroczynska, Michele Carbone

2979 related Products with: Cross reactivity between many anti-human antibodies for their hamster homologs provide the tools to study the signal transduction pathway activated by asbestos and SV40 in the malignant mesothelioma model.

100 μg1mg100ug/vial1 ml100 100 μg1 ml100

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#10535755   // To Up

Nuclear vitamin K2 binding protein in human osteoblasts: homologue to glyceraldehyde-3-phosphate dehydrogenase.

The importance of vitamin K in bone metabolism has been suggested previously. The binding protein of vitamin K2 (menatetrenone, 2-methyl-3-all-trans-tetraphenyl-1,4-naphthoquinone, menaquinone-4), found in nuclear extract of human osteoblasts, binds to vitamin K1 and K2, but not K3. Since the binding protein does not bind to other steroids or vitamins, such as hydrocortisone, vitamin A, 1,25(OH)2vitamin D3, trolox (a derivative of vitamin E), and warfarin, a specific binding protein to vitamin K1 and vitamin K2 in osteoblasts was suggested. The size of the specific binding protein was revealed to be 6S by sucrose density gradient and about 40,000 daltons by SDS-PAGE. Twenty amino acid residues from the N-terminal were the same as human glyceraldehyde-3-phosphate dehydrogenase (GAPDH), but the 21st residue, alanine, was replaced with serine. The binding protein was precipitated with anti-human GAPDH antibody, and authentic human GAPDH could bind vitamin K2. We propose that the nuclear binding protein for vitamin K2 exists in nuclei similarly to other vitamin receptors and that the molecular structure is very close to human GAPDH.
K Hoshi, K Nomura, Y Sano, Y Koshihara

1564 related Products with: Nuclear vitamin K2 binding protein in human osteoblasts: homologue to glyceraldehyde-3-phosphate dehydrogenase.

100 μg100 100 UG1mg100 μg100 100 μg 100ul25 1 kit(96 Wells)2ug 100ul

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