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Guanylurea+phosphate


9,068  results were found

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Supplier:  Bioss
Description:   GOT1L1, Glutamate oxaloacetate transaminase 1-like protein 1, is a 421 amino acid member of the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to glutamate-oxaloacetate transaminase (GOT1), GOT1L1 is found primarily as a homodimer in the cytoplasmic space but also has mitochondrial and chloroplastic isozymes. GOT1L1 transaminates 2-oxoglutarate with L-aspartate to yield oxaloacetate and L-glutamate. This reaction requires a pyridoxal phosphate cofactor to occur. The GOT1L1 peptidase is predominately expressed in the liver and serum levels of this protein can be used as an indicator of liver disease. Also, elevated glutamate concentrations in the brain interstitial fluids can lead to pathological brain conditions. The glutamate-scavenging properties of these aminotranferase type enzymes likely prevent glutamate excitotoxicity and the long-lasting neurological deficits seen after stroke.
Catalog Number: (76071-158)

Supplier:  Prosci
Description:   TPI1, Polyclonal Antibody, Host: Rabbit, Species Reactivity: Human, Mouse, Immunogen: conjugated synthetic peptide between 68-96 amino acids from the N-terminal region, Isotype: Ig, Synonym: Triose-phosphate isomerase, TPI1
Catalog Number: (10109-544)

Supplier:  Prosci
Description:   Adenylate kinases are involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. Three isozymes of adenylate kinase, namely 1, 2, and 3, have been identified in vertebrates. Expression of these isozymes is tissue-specific and developmentally regulated. Isozyme 2 is localized in the mitochondrial intermembrane space and may play a role in apoptosis.Adenylate kinases are involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. Three isozymes of adenylate kinase, namely 1, 2, and 3, have been identified in vertebrates; this gene encodes isozyme 2. Expression of these isozymes is tissue-specific and developmentally regulated. Isozyme 2 is localized in the mitochondrial intermembrane space and may play a role in apoptosis. Two transcript variants encoding distinct isoforms have been identified for this gene.
Catalog Number: (RL001-0933)

Supplier:  Rockland Immunochemical
Description:   1mg. Antibody Concentration: 1 mg/mL. Fluorochrome/Protein Ratio: 4.3 moles Texas Red per mole of bovine serum albumin. Buffer: 0.02M potassium phosphate, 0.15M sodium chloride, pH 7.2. Stabilizer: 10 mg/mL polyethylene glycol (PEG-8000). Lyophilized.
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Supplier:  Prosci
Description:   Creatine kinases (CK) are a large family of isoenzymes that regulate levels of ATP in subcellular compartments, where they provide ATP at sites of fluctuating energy demand by the transfer of phosphates between creatine and adenine nucleotides. CKs provide the energy of phosphate hydrolysis necessary to drive the normal function of many cellular systems. In cells, the cytosolic CK enzymes consist of two subunits, which can be either B (brain type) or M (muscle type). There are three different isoenzymes: CKMM, CKBB and CKMB. This mAb recognizes the CKBB isoenzyme and does not react with the B subunit in CKMB. It shows minimal reactivity with other human serum proteins
Catalog Number: (10071-710)

Supplier:  Prosci
Description:   UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. It is involved in the pathway of nucleotide and deoxyribonucleotide catabolism.
Supplier:  Bioss
Description:   DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. May also act as a negative regulator of ETS1 and may inhibit nuclear factor-kappa-B activation.
Supplier:  Bioss
Description:   DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. May also act as a negative regulator of ETS1 and may inhibit nuclear factor-kappa-B activation.

Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Catalog Number: (10412-736)

Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Catalog Number: (10413-200)

Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

Supplier:  Bioss
Description:   The inositol polyphosphate 5-phosphatases selectively remove the phosphate from the 5-position of various phosphatidylinositols, which generate second messengers in response to extracellular signals. Synaptojanins are characterized by an N-terminal SAC1-like sequence, a central 5-phosphate domain, and a unique C-terminal sequence and have been shown to use phosphatidylinositol 4,5-bisphosphate as a substrate. Synaptojanins exist as two isoforms, synaptojanin 1 and 2, which differ in the C-terminal domain, and each isoform has multiple variants produced by alternative splicing. Synaptojanin 1 is expressed as two major forms: the shorter is found in brain while the longer is expressed in peripheral tissues. Eight splice variants of synaptojanin 2 have been detected, including a brain specific isoform. Synaptojanins are thought to participate in the endocytosis of synaptic vesicles and the regulation of the actin cytoskeleton.

Supplier:  Bioss
Description:   The inositol polyphosphate 5-phosphatases selectively remove the phosphate from the 5-position of various phosphatidylinositols, which generate second messengers in response to extracellular signals. Synaptojanins are characterized by an N-terminal SAC1-like sequence, a central 5-phosphate domain, and a unique C-terminal sequence and have been shown to use phosphatidylinositol 4,5-bisphosphate as a substrate. Synaptojanins exist as two isoforms, synaptojanin 1 and 2, which differ in the C-terminal domain, and each isoform has multiple variants produced by alternative splicing. Synaptojanin 1 is expressed as two major forms: the shorter is found in brain while the longer is expressed in peripheral tissues. Eight splice variants of synaptojanin 2 have been detected, including a brain specific isoform. Synaptojanins are thought to participate in the endocytosis of synaptic vesicles and the regulation of the actin cytoskeleton.

Supplier:  Bioss
Description:   GOT1L1, Glutamate oxaloacetate transaminase 1-like protein 1, is a 421 amino acid member of the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to glutamate-oxaloacetate transaminase (GOT1), GOT1L1 is found primarily as a homodimer in the cytoplasmic space but also has mitochondrial and chloroplastic isozymes. GOT1L1 transaminates 2-oxoglutarate with L-aspartate to yield oxaloacetate and L-glutamate. This reaction requires a pyridoxal phosphate cofactor to occur. The GOT1L1 peptidase is predominately expressed in the liver and serum levels of this protein can be used as an indicator of liver disease. Also, elevated glutamate concentrations in the brain interstitial fluids can lead to pathological brain conditions. The glutamate-scavenging properties of these aminotranferase type enzymes likely prevent glutamate excitotoxicity and the long-lasting neurological deficits seen after stroke.
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