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AB159891

Recombinant Human PXDN/VPO1 protein (GST tag N-Terminus)

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Recombinant Human PXDN/VPO1 protein (GST tag N-Terminus) is a Human Fragment protein, in the 1452 to 1561 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

KIAA0230, MG50, PRG2, PXD01, VPO, VPO1, PXDN, Peroxidasin homolog, Melanoma-associated antigen MG50, Peroxidasin 1, Vascular peroxidase 1, p53-responsive gene 2 protein, hsPxd01

1 Images
SDS-PAGE - Recombinant Human PXDN/VPO1 protein (GST tag N-Terminus) (AB159891)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human PXDN/VPO1 protein (GST tag N-Terminus) (AB159891)

ab159891 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q92626

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product was previously labelled as PXDN.
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Sequence info

[{"sequence":"STSAFSTRSDASGTNDFREFVLEMQKTITDLRTQIKKLESRLSTTECVDAGGESHANNTKWKKDACTICECKDGQVTCFVEACPPATCAVPVNIPGACCPVCLQKRAEEK","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":1561,"aminoAcidStart":1452,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q92626","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PXDN also known as VPO1 functions as a peroxidase enzyme with a mass of approximately 180 kDa. It catalyzes the oxidation of halide and thiocyanate ions using hydrogen peroxide. This action results in the production of hypohalous acids. PXDN is widely expressed in tissues including heart lung liver and kidney. It plays essential roles in the extracellular matrix by influencing the formation of collagen cross-links.
Biological function summary

Peroxidase activity from PXDN contributes significantly to tissue development and wound healing processes. PXDN participates in forming dityrosine bonds which contribute to the structural stability of basement membranes. The protein can function as part of larger molecular complexes which enhances its ability to interact within various biochemical environments. Its role in tissue repair aligns with these complex interactions highlighting its involvement in maintaining tissue integrity.

Pathways

Peroxidase activity from PXDN participates in the oxidative stress response and extracellular matrix organization. In the oxidative stress response pathway PXDN involves modulation of reactive oxygen species interacting with other proteins like glutathione peroxidase to mitigate cellular damage. During extracellular matrix organization PXDN supports latent transforming growth factor-beta-binding protein-mediated stabilization of growth factors required for matrix remodeling.

PXDN's dysregulation has associations with cancer and fibrotic conditions. Its abnormal expression or activity levels can contribute to malignancies through imbalanced cell signaling and extracellular matrix disorganization. In the context of fibrosis PXDN connects with proteins like fibronectin influencing abnormal tissue remodeling and excessive deposition of extracellular matrix components. Understanding these associations offers potential for therapeutic targeting of PXDN in related disease processes.
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Specifications

Form

Liquid

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General info

Function

Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer (PubMed : 18929642, PubMed : 19590037, PubMed : 22842973, PubMed : 25708780, PubMed : 25713063, PubMed : 27697841, PubMed : 28154175, PubMed : 34679700). In turns, directly contributes to the collagen IV network-dependent fibronectin/FN and laminin assembly, which is required for full extracellular matrix (ECM)-mediated signaling (PubMed : 19590037, PubMed : 32543734, PubMed : 34679700). Thus, sulfilimine cross-links are essential for growth factor-induced cell proliferation and survival in endothelial cells, an event essential to basement membrane integrity (PubMed : 32543734). In addition, through the bromide oxidation, may promote tubulogenesis and induce angiogenesis through ERK1/2, Akt, and FAK pathways (PubMed : 25713063). Moreover brominates alpha2 collagen IV chain/COL4A2 at 'Tyr-1485' and leads to bromine enrichment of the basement membranes (PubMed : 32571911). In vitro, can also catalyze the two-electron oxidation of thiocyanate and iodide and these two substrates could effectively compete with bromide and thus inhibit the formation of sulfilimine bonds (PubMed : 28154175). Binds laminins (PubMed : 32485152). May play a role in the organization of eyeball structure and lens development during eye development (By similarity).

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Post-translational modifications

Glycosylated (PubMed:25713063). Four sites are completely N-glycosylated (Asn-640, Asn-731, Asn-865 and Asn-1425), whereas the others are found partially glycosylated (PubMed:25713063).. Processed by FURIN and the proteolytic processing largely depends on the peroxidase activity of PXDN (PubMed:27697841, PubMed:34679700). The proteolytic cleavage occurs after intracellular homotrimerization and releases into the extracellular matrix a large, catalytically active fragment and a smaller fragment consisting primarily of the C-terminal VWFC domain (PubMed:27697841, PubMed:31295557). The processing enhances both peroxidase activity and sulfilimine cross-links formation (PubMed:27697841, PubMed:34679700).

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Product protocols

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Target data

Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer (PubMed : 18929642, PubMed : 19590037, PubMed : 22842973, PubMed : 25708780, PubMed : 25713063, PubMed : 27697841, PubMed : 28154175, PubMed : 34679700). In turns, directly contributes to the collagen IV network-dependent fibronectin/FN and laminin assembly, which is required for full extracellular matrix (ECM)-mediated signaling (PubMed : 19590037, PubMed : 32543734, PubMed : 34679700). Thus, sulfilimine cross-links are essential for growth factor-induced cell proliferation and survival in endothelial cells, an event essential to basement membrane integrity (PubMed : 32543734). In addition, through the bromide oxidation, may promote tubulogenesis and induce angiogenesis through ERK1/2, Akt, and FAK pathways (PubMed : 25713063). Moreover brominates alpha2 collagen IV chain/COL4A2 at 'Tyr-1485' and leads to bromine enrichment of the basement membranes (PubMed : 32571911). In vitro, can also catalyze the two-electron oxidation of thiocyanate and iodide and these two substrates could effectively compete with bromide and thus inhibit the formation of sulfilimine bonds (PubMed : 28154175). Binds laminins (PubMed : 32485152). May play a role in the organization of eyeball structure and lens development during eye development (By similarity).
See full target information PXDN
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