Prolyl 4-hydroxylase (P4-H), an enzyme localized to the endoplasmi reticulum (ER), catalyses the co- and post-translational hydroxylation of proline residues in Xaa-Pro-Gly sequences of collagens and proteins with collagen-like aa sequences. Vertebrate P4-H consists of two distinct polypeptides; the catalytically more important, glycosylated alpha-subunit (64kD) and the beta-subunit (60kD) which belongs to the multifunctional enzyme protein disulphide isomerase (PDI). The beta subunit is a major cellular thyroid hormone-binding protein and shows partial homology with a phosphoinositide-specific phospholipase C, thioredoxins, and the estrogen-binding domain of the estrogen receptor.It catalyzes the formation, breakage and rearrangement of disulfide bonds. It also acts as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner at high concentrations. Other function of the protein includes its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex. The COOH-terminus of the beta subunit has the aa sequence Lys-Asp-Glu-Leu, which was recently suggested to be necessary for the retention of a polypeptide within the lumen of the endoplasmic reticulum.
Applications:
Suitable for use in Immunohistochemistry. Other applications not tested.
Recommended Dilution:
Immunohistochemistry (formalin fixed paraffin embedded): 1:25-1:50
Optimal dilutions to be determined by the researcher.
Positive Control:
Thymus
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Quick Search
Products 
