You Searched For: N-Acetyl-L-hydroxyproline


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Catalog Number: (BOSSBS-3686R-A647)
Supplier: Bioss
Description: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferencially recognized via a LXXLAP motif.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3686R-A488)
Supplier: Bioss
Description: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferencially recognized via a LXXLAP motif.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3686R-HRP)
Supplier: Bioss
Description: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferencially recognized via a LXXLAP motif.
UOM: 1 * 100 µl


Supplier: Merck
Description: trans-4-Hydroxy-L(-)-proline, Sigma-Aldrich®

Supplier: Merck
Description: cis-4-Hydroxy-L-(-)-proline, Sigma-Aldrich®

Catalog Number: (ROTH3893.1)
Supplier: Roth Carl
Description: trans-4-Hydroxy-L(-)-proline
UOM: 1 * 5 g


Catalog Number: (MOLEM32560054)
Supplier: Molekula
Description: cis-4-Hydroxy-D(+)-proline
UOM: 1 * 1 g


Catalog Number: (BEHRB00218426)
Supplier: BEHR
Description: This six sample digestion apparatus with energy control is suitable for determination of hydroxyproline content.
UOM: 1 * 1 items


Catalog Number: (SIALH5877-10G)
Supplier: Merck
Description: cis-4-Hydroxy-D(+)-proline, Sigma-Aldrich®
UOM: 1 * 10 g


Catalog Number: (HEWL5062-2478)
Supplier: Agilent
Description: A kit with amino acid standards (17 components) at different concentrations together with reagents and buffers required for analysis.
UOM: 1 * 1 items


Catalog Number: (MOLE45298012-25G)
Supplier: Molekula
Description: trans-4-Hydroxy-L(-)-proline
UOM: 1 * 25 g


Supplier: Merck
Description: trans-4-Hydroxy-L(-)-proline, Sigma-Aldrich®

Supplier: Merck
Description: trans-4-Hydroxy-L(-)-proline, Sigma-Aldrich®

Catalog Number: (PRSI92-214)
Supplier: ProSci Inc.
Description: PEPD belongs to the peptidase M24B family of Eukaryotic-type prolidase subfamily. PEPD is a cytosolic dipeptidase that hydrolyses dipeptides with proline or hydroxyproline at the carboxy terminus. It is important in collagen metabolism because of the high levels of imino acids. Defects in PEPD are a cause of prolidase deficiency which is an autosomal recessive disorder associated with iminodipeptiduria.
UOM: 1 * 50 µG


Catalog Number: (PRSI27-081)
Supplier: ProSci Inc.
Description: Xaa-Pro dipeptidase is a cytosolic dipeptidase that hydrolyzes dipeptides with proline or hydroxyproline at the carboxy terminus (but not Pro-Pro). It is important in collagen metabolism because of the high levels of iminoacids.Xaa-Pro dipeptidase is a cytosolic dipeptidase that hydrolyzes dipeptides with proline or hydroxyproline at the carboxy terminus (but not Pro-Pro). It is important in collagen metabolism because of the high levels of iminoacids. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
UOM: 1 * 50 µG


Supplier: Thermo Fisher Scientific
Description: (2S,3S)-3-Hydroxypyrrolidine-2-carboxylic acid

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