Recombinant Human P4HA1 protein is a Human Full Length protein, in the 1 to 534 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
P4HA, P4HA1, Prolyl 4-hydroxylase subunit alpha-1, 4-PH alpha-1
Recombinant Human P4HA1 protein is a Human Full Length protein, in the 1 to 534 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.3% Glutathione
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Belongs to the P4HA family.
The protein P4HA1 also known as Prolyl 4-Hydroxylase Subunit Alpha 1 functions mechanically by catalyzing the hydroxylation of proline residues in collagen. This activity requires iron and ascorbate as cofactors. P4HA1 is a part of the prolyl 4-hydroxylase enzyme complex and contains a molecular mass of approximately 63 kDa. It expresses widely in various human tissues with high expression in the liver skin and vascular tissues reflecting its role in collagen synthesis.
P4HA1 plays a central role in collagen biosynthesis and maturation by introducing hydroxyl groups into proline residues which stabilize the collagen triple helix. This protein functions as a critical component of the prolyl 4-hydroxylase complex which includes a beta subunit. Proper formation and stability of collagen fibers depend on P4HA1 activity impacting the structural integrity of connective tissues throughout the body.
P4HA1's function integrates into the pathways of collagen biosynthesis and modification. It is significant in the extracellular matrix organization pathway which upholds the structural support and cellular signaling. Additionally P4HA1 interacts with other proteins like COL1A1 and PLOD1 during these processes assisting in the proper formation of extracellular matrix structures essential for tissue function and injury repair.
P4HA1 has a strong association with fibrotic diseases such as liver fibrosis and pulmonary fibrosis where excessive collagen deposition is a hallmark. Dysregulation of P4HA1 may also play a role in tumor progression in cancers by promoting extracellular matrix remodeling therefore facilitating tumor invasion and metastasis. The protein interacts with pathways involving vascular endothelial growth factor (VEGF) which drives angiogenesis and is implicated in these disease processes.
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ab114624 analysed on a 12.5% SDS-PAGE stained with Coomassie Blue.
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