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P4HA1 encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. Additionally we are shipping P4HA1 Antibodies (60) and P4HA1 Kits (19) and many more products for this protein.
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Overexpression of P4Ha1 increased atherosclerotic plaque size.
IL-6 (show IL6 Proteins) destabilizes atherosclerotic plaques by downregulating P4Halpha1 via an RAF-MEK1/2-ERK1/2 MAPK and c-Jun pathway.
C-P4H alpha(I) and alpha(II (show GSTA3 Proteins)) mRNA levels were increased in hypoxic mouse chondrocytes in a manner dependent on HIF-1a (show HIF1A Proteins).
we report compound heterozygous frameshift and splice site mutations in P4HA1 that impair but not abolish C-P4H alpha(I) activity. The maternal P4HA1 exon 12 splice donor site mutation causes an internally deleted C-P4H alpha(I) predicted to completely lack catalytic activity. two nucleic acid insertion in exon 9 results in a premature stop in the exon 9 P4HA1 splice form.
Findings suggest that the catalytic domain of collagen prolyl 4-hydroxylases (CP4Hs) recognizes the cis (show CISH Proteins) conformation of the prolyl peptide bond.
Thus, we conclude that miR (show MLXIP Proteins)-30e suppresses proliferation of hepatoma cells through targeting P4HA1 mRNA.
Studies indicate P4HA1 copy number gain in a subset of metastatic prostate tumors and its expression is also regulated by microRNA-124.
Overexpression of miR (show MLXIP Proteins)-122 markedly attenuated the expression of P4HA1 via targeting a binding site located at 3'-UTR of P4HA1 mRNA
Hypoxia-inducible factor 1 (HIF-1 (show HIF1A Proteins)) promotes extracellular matrix remodeling under hypoxic conditions by inducing P4HA1, P4HA2 (show P4HA2 Proteins), and PLOD2 (show PLOD2 Proteins) expression in fibroblasts.
IL-6 (show IL6 Proteins) significantly downregulated P4Halpha1 expression in aortic smooth muscle cells
analysis of the 2-His-1 (show HTN1 Proteins)-Asp (show ASIP Proteins) active-site motif in prolyl 4-hydroxylase
Collagen prolyl 4-hydroxylase-alpha (I)mRNA is stabilized by interation of RNA-binding proteins hnRNP-A2/B1 with a U(16) element within the 3'-UTR
Results suggest that the alteration of translational efficiency by nucleolin (show NCL Proteins), which occurs through a hypoxia inducible factor independent pathway, is an important step in collagen prolyl 4-hydroxylase-alpha(I) regulation under hypoxia.
This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. The encoded protein is one of several different types of alpha subunits and provides the major part of the catalytic site of the active enzyme. In collagen and related proteins, prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline that is essential to the proper three-dimensional folding of newly synthesized procollagen chains. Alternatively spliced transcript variants encoding different isoforms have been described.
prolyl 4-hydroxylase subunit alpha-1
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide I
, prolyl 4-hydroxylase alpha subunit
, prolyl 4-hydroxylase, alpha I subunit
, 4-PH alpha-1
, procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
, collagen prolyl 4-hydroxylase alpha(I)
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha 1 polypeptide