Monoclonal Anti-PXDN antibody produced in mouse

Drosophila peroxidasin is an extracellular matrix-associated peroxidase (Horikoshi et al., 1999 [PubMed 10441517]). It is expressed exclusively in hemocytes derived from head mesoderm at a very early stage of differentiation. Peroxidasin exists as a homotrimer with a unique hybrid structure that combines an enzymatically functional peroxidase domain with motifs that are typically found in extracellular matrix-associated proteins. It is a secreted protein that contains a secretory recognition sequence at its N terminus. Peroxidasin catalyzes hydrogen peroxide-driven radioiodination, oxidations, and the formation of dityrosine in vitro. It is also thought to function in extracellular matrix consolidation, phagocytosis, and defense.[supplied by OMIM] Peroxidasin (PXDN) is a multidomain, glycosylated, homotrimeric peroxidase. It is expressed in the endoplasmic reticulum and secreted into the extracellular matrix. The 1479-amino acid protein belongs to the peroxidase-cyclooxygenase superfamily. It possesses a catalytic peroxidase domain (POX), a leucine-rich repeat domain (LRR), four C-like immunoglobulin domains (Ig) at the amino-terminal and a carboxy-terminal von Willebrand factor type C module (VWC). The gene encoding PXDN has 23 exons and is localized on human chromosome 2p25.3.

PXDN (XP_056455, 1452 a.a. ~ 1561 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
STSAFSTRSDASGTNDFREFVLEMQKTITDLRTQIKKLESRLSTTECVDAGGESHANNTKWKKDACTICECKDGQVTCFVEACPPATCAVPVNIPGACCPVCLQKRAEEK

Peroxidasin (PXDN) releases hypobromous acid, which is involved in collagen IV reinforcement. The protein stabilizes the basement membrane by enhancing the covalent crosslinks in the collagen IV network. Mutations in the gene encoding PXDN have been linked to microphthalmia and anterior segment dysgenesis.

Solution in phosphate buffered saline, pH 7.4

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