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Merck

SAB1402973

Sigma-Aldrich

Monoclonal Anti-PXDN antibody produced in mouse

clone 2C11, purified immunoglobulin, buffered aqueous solution

别名:

D2S448, D2S448E, KIAA0230, MG50, PRG2, PXN, VPO

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

mouse

共軛

unconjugated

抗體表格

purified immunoglobulin

抗體產品種類

primary antibodies

無性繁殖

2C11, monoclonal

形狀

buffered aqueous solution

分子量

antigen ~38.21 kDa

物種活性

human

技術

capture ELISA: suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL

同型

IgG2bκ

NCBI登錄號

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... PXDN(7837)

一般說明

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.

免疫原

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

生化/生理作用

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.

外觀

Solution in phosphate buffered saline, pH 7.4

免責聲明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Jodi Dougan et al.
International journal of molecular sciences, 20(12) (2019-06-27)
Peroxidasin (PXDN), a human homolog of Drosophila PXDN, belongs to the family of heme peroxidases and has been found to promote oxidative stress in cardiovascular tissue, however, its role in prostate cancer has not been previously elucidated. We hypothesized that
Microduplications Disrupting the MYT1L Gene (2p25.3) are Associated with Schizophrenia
Yohan Lee
Psychiatric Genetics (2012)
Selene Colon et al.
American journal of physiology. Renal physiology, 316(2), F360-F371 (2018-12-20)
Renal fibrosis is the pathological hallmark of chronic kidney disease (CKD) and manifests as glomerulosclerosis and tubulointerstitial fibrosis. Reactive oxygen species contribute significantly to renal inflammation and fibrosis, but most research has focused on superoxide and hydrogen peroxide (H2O2). The
Novel mutations in PXDN cause microphthalmia and anterior segment dysgenesis.
Choi A
European Journal of Human Genetics (2015)
Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1.
Paumann-Page M
The Journal of Biological Chemistry (2017)

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