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HPA019616

Sigma-Aldrich

Anti-LPAR2 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

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Synonym(s):
Anti-LPA receptor 2, Anti-LPA-2, Anti-Lysophosphatidic acid receptor 2, Anti-Lysophosphatidic acid receptor Edg-4
UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

technique(s)

immunohistochemistry: 1:20- 1:50

immunogen sequence

LLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDAEMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... LPAR2(9170)

General description

LPAR2 (Lysophosphatidic acid receptor 2) is a bioactive lysophospholipid belonging to the endothelial cell differentiation gene (EDG) family of GPCRs. It is widely expressed in different tissues and cell types.

Immunogen

Lysophosphatidic acid receptor 2 recombinant protein epitope signature tag (PrEST)

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)

Biochem/physiol Actions

LPAR2 (Lysophosphatidic acid receptor 2) is involved in various downstream signaling pathways such as RhoA-ROCK and STAT-3 signaling. It plays a key role in the colorectal cancer (CRC) pathology. In CRC progression it controls cell cycle progression, migration, invasion, and proliferation. During cell migration, it has been reported that cell-cell binding ability depends on the internalization of N-cadherin downstream of lysophosphatidic acid (LPA) receptor 2. LPAR2 is also associated with the receptor-mediated phospholipase C-β3 activation. During activation, C-terminal PDZ domain-binding motif of LPAR2 directly binds to the second PDZ domain of Na(+)/H(+) exchanger regulatory factor2 (NHERF2). Later, that LPAR2 linked PDZ domain of NHERF2 binds to PLC-β3 and forms a complex, which is responsible for gene silencing of PLC-β3.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST72734

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

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.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

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Yong-Seok Oh et al.
Molecular and cellular biology, 24(11), 5069-5079 (2004-05-15)
Lysophosphatidic acid (LPA) activates a family of cognate G protein-coupled receptors and is involved in various pathophysiological processes. However, it is not clearly understood how these LPA receptors are specifically coupled to their downstream signaling molecules. This study found that
Sei Kuriyama et al.
The Journal of cell biology, 206(1), 113-127 (2014-07-09)
Collective cell migration (CCM) and epithelial-mesenchymal transition (EMT) are common to cancer and morphogenesis, and are often considered to be mutually exclusive in spite of the fact that many cancer and embryonic cells that have gone through EMT still cooperate
Shigeru Hashimoto et al.
Nature communications, 7, 10656-10656 (2016-02-09)
Acquisition of mesenchymal properties by cancer cells is critical for their malignant behaviour, but regulators of the mesenchymal molecular machinery and how it is activated remain elusive. Here we show that clear cell renal cell carcinomas (ccRCCs) frequently utilize the
Fernanda Leve et al.
PloS one, 10(9), e0139094-e0139094 (2015-09-30)
Lysophosphatidic acid (LPA) plays a critical role in the proliferation and migration of colon cancer cells; however, the downstream signaling events underlying these processes remain poorly characterized. The aim of this study was to investigate the signaling pathways triggered by

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