4060 Results for: "JACOB COWEN &amp"

Supplier: JACOB COWEN AND SONS

These non-absorbent bleached cotton wool rolls are made of 100% cotton.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterised by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Biosensis

14.3.3 protein eta or 14.3.3  binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (Ref SwissProt). 14.3.3 protein eta is widely expressed as both homodimers and heterodimers and are concentrated in the nervous system. High concentrations of 14.3.3 protein eta have been linked to Creutzfeld Jacob Disease, Parkinson's Disease and early-onset schizopherenia.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterised by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Bioss

Prion diseases or transmissible spongiform encephalopathies (TSEs) are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Infectious PrPSc is highly expressed in the brain of animals affected by TSEs, including scrapie in sheep, BSE in cattle, and Cruetzfeldt-Jacob disease in humans. The PRND gene locus, located on human chromosome 20p, encodes for the doppel protein (Dpl), which exhibits approximately 25% sequence homology with PrP. Dpl is characterized by an alpha-helical conformation, intramolecular disulfide bonds, and two N-linked oligosaccharides, and it is presented on the cell surface by a glycosylphosphatidylinositol anchor. Dpl is highly expressed in adult testis and heart and is detectable in the brain of neonatal mice. Dpl does not appear to contribute to prion disease progression, but ectopic expression of Dpl is implicated in neuronal degeneration of ataxic PRP-deficient mice. Dpl is also thought to play a role in angiogenesis, specifically maturation of the blood-brain barrier.

Supplier: Aesculap

Uterine tenaculum forceps, Tissue forceps, Design according to: Jacobs, 215 mm

Supplier: Merck

AMP (2-Amino-2-methylpropanol) for synthesis, Sigma-Aldrich®

Supplier: VWR Chemicals

5% water has been added to maintain liquidity at room temperature.

Supplier: Thermo Fisher Scientific

Adenosine-5'-monophosphoric acid (AMP) 99%

Supplier: Thermo Fisher Scientific

AMP (2-Amino-2-methylpropanol) 99%

Supplier: Thermo Fisher Scientific

AMP (2-Amino-2-methylpropanol), (max. 5% H₂O) 95%

Supplier: Merck

2-Acrylamido-2-methylpropanesulphonic acid for synthesis, Sigma-Aldrich®

Supplier: ENZO LIFE SCIENCES

Adenosine 5'-monophosphate disodium salt (AMP disodium salt) ≥98% (by HPLC)

Supplier: ENZO LIFE SCIENCES

Amp'd® ELISA Signal Amplification Kit provides up to 50-fold increase in sensitivity over traditional ELISAs while detecting lower concentrations of target in samples.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: US Biological

Anti-Cyclic AMP Rabbit Polyclonal Antibody

Supplier: ENZO LIFE SCIENCES

Rifampicin

Supplier: ENZO LIFE SCIENCES

Ultra-sensitive AMP'D® GLP-1 ELISA kit enabling the ability to use less sample to detect levels of human Glucagon-like peptide 1 (7-36) amide, a potent promoter of insulin secretion, a major incretin hormone, and therapeutic for type 2 diabetes.

Supplier: US Biological

Anti-AMP Activated Protein Kinase alpha1/2 Mouse Monoclonal Antibody [clone: 9E22]