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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.
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Overexpression of P4Ha1 increased atherosclerotic plaque size.
IL-6 (zeige IL6 Proteine) 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 (zeige GSTA3 Proteine)) mRNA levels were increased in hypoxic mouse chondrocytes in a manner dependent on HIF-1a (zeige HIF1A Proteine).
Our study indicates that P4HA1 plays a pivotal role in the process of GSC (zeige GSC Proteine)-EC transdifferentiation and the structural formation of vascular BMs.
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 (zeige CISH Proteine) conformation of the prolyl peptide bond.
Thus, we conclude that miR (zeige MLXIP Proteine)-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 (zeige MLXIP Proteine)-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 (zeige HIF1A Proteine)) promotes extracellular matrix remodeling under hypoxic conditions by inducing P4HA1, P4HA2 (zeige P4HA2 Proteine), and PLOD2 (zeige PLOD2 Proteine) expression in fibroblasts.
IL-6 (zeige IL6 Proteine) significantly downregulated P4Halpha1 expression in aortic smooth muscle cells
analysis of the 2-His-1 (zeige HTN1 Proteine)-Asp (zeige ASIP Proteine) 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
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