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Lead Time
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Usage
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation.
Gene References into Functions
The results indicate that LPA2 and LPA3 receptors play opposing roles during red blood cells differentiation. PMID: 27244685
These results suggest that LPA signaling via LPA2 may play an important role in the regulation of cellular functions in HT1080 cells treated with cisplatin. PMID: 28205098
LPA2 mRNA levels were associated with poorer differentiation, and higher LPA6 levels were associated with microvascular invasion in HCC; both became a risk factor for recurrence after surgical treatment when combined with increased serum ATX levels PMID: 27583415
epithelial dysplasia was observed in founder mouse intestine, correlating LPA2 overexpression with epithelial dysplasia. The current study demonstrates that overexpression of LPA2 alone can lead to intestinal dysplasia. PMID: 27124742
LPA2 expression was associated with HIF-1alpha expression and that a high level of LPA2 was associated with shorter overall survival and was an independent prognostic predictor for breast cancer in Chinese women. PMID: 27805252
LPAR2 mRNA is up-regulation in colorectal cancer. PMID: 26937138
Data show high expression levels of LPAR2 and LPAR1 in endometrial cancer tissue with positive correlations with FIGO stage suggesting them as potential biomarkers for endometrial cancer progression. PMID: 26327335
Suggest that LPA2 and LPA3 may function as a molecular switch and play opposing roles during megakaryopoiesis of K562 cells. PMID: 25463482
the RhoA-regulated formin Dia1 is involved in entosis downstream of LPAR2 PMID: 24950964
Crystal structure of NHERF2 PDZ1 domain complex with C-terminal LPA2 sequence. The PDZ1-LPA2 binding specificity is achieved by hydrogen bonds and hydrophobic contacts with the last four LPA2 residues contributing to specific interactions. PMID: 24613836
LPA1 and LPA2 are major LPA receptor subtypes compared with low-expressed LPA3 in PANC-1 tumor cells. PMID: 24061591
Lysophosphatidic acid (LPA) increased hepatocellular carcinoma cells cell invasion, which was LPA-receptor dependent. PMID: 23569130
LPA2 and LPA6 receptor subtypes are predominant in both HPAECs and HMVECs PMID: 23084965
found that LPA receptor 2/3-mediated IL-8 expression occurs through Gi/PI3K/AKT, Gi/PKC and IkappaB/NF-kappaB signaling PMID: 21964883
This work shows for the first time that key components of the LPA pathway are modulated following traumatic brain injuries in humans. PMID: 21234797
MAGI-3 competes with NHERF-2 to negatively regulate LPA2 receptor signaling in colon cancer cells. PMID: 21134377
LPA2 gene mutation may play some role in the pathogenesis of colon cancer. PMID: 20890765
show that human microglia express LPA receptor subtypes LPA(1), LPA(2), and LPA(3) on mRNA and protein level. LPA activation of C13NJ cells induced Rho and extracellular signal-regulated kinase activation and enhanced cellular ATP production. PMID: 19899077
demonstrate that two biological fluids, blood plasma and seminal plasma, differentially activate LPA receptors PMID: 12123830
results suggested that LPA(2) and LPA(3) may be involved in VEGF expression mediated by LPA signals in human ovarian oncogenesis PMID: 12668280
LPA may directly increase the level of cyclin D1 in ovarian cancer cells, increasing their proliferation. PMID: 12759391
Upregulation of LPA2 may play a role in carcinogenesis, particularly in postmenopausal breast cancer. PMID: 15535846
LPA2 is the major LPA receptor in colon cancer cells and cellular signals by LPA2 are largely mediated through its ability to interact with NHERF2. PMID: 15728708
formation of the LPA receptor/PDZ domain-containing RhoGEF complex plays a pivotal role in LPA-induced RhoA activation PMID: 15755723
These results demonstrate that MAGI-3 interacts directly with LPA(2) and regulates the ability of LPA(2) to activate Erk and RhoA. PMID: 16904289
EDG4 and EDG2 cooperate to promote LPA-stimulated chemotaxis in breast tumor cell lines. PMID: 17496233
data suggest that LPA receptor-dependent expression of CTGF and CYR61 represents a common host response after interaction with bacteria. PMID: 17765657
lysophosphatidic acid 2 receptor mediates down-regulation of Siva-1 to promote cell survival PMID: 17965021
A role for the transgenic lysophosphatidic acid (LPA)2 receptor is identified in regulating smooth muscle cell migratory responses in the context of vascular injury. PMID: 18703779
LPA and LPA receptors, LPA(2) as well as LPA(1), represent potential therapeutic targets for patients with MPM PMID: 18754873
Expression of LPA2 during ovarian carcinogenesis contributes to ovarian cancer aggressiveness, suggesting that the targeting of LPA production and action may have potential for the treatment of ovarian cancer. PMID: 19001604
Switching of LPA receptor expression from LPA3 to LPA1, may be involved in prostate cancer progression and/or androgen independence PMID: 19025891
LPA(1) receptor, LPA(2) and LPA(3) receptors-induced VASP phosphorylation is a critical mediator of tumor cell migration initiation PMID: 19081821
LPA2 and Gi/Src pathways are significant for LPA-induced COX-2 expression and cell migration that could be a promising drug target for ovarian cancer cell metastasis. PMID: 19116446
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Subcellular Location
Cell surface. Cell membrane; Multi-pass membrane protein. Note=Prior to LPA treatment found predominantly at the cell surface but in the presence of LPA colocalizes with RALA in the endocytic vesicles.
Protein Families
G-protein coupled receptor 1 family
Tissue Specificity
Expressed most abundantly in testes and peripheral blood leukocytes with less expression in pancreas, spleen, thymus and prostate. Little or no expression in heart, brain, placenta, lung, liver, skeletal muscle, kidney, ovary, small intestine, or colon.