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AB145226

BML 280, PLD2 inhibitor

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(1 Publication)

MW 429.5 Da, Purity >98%. Potent, selective PLD2 inhibitor (IC50 values are 90 and 500 nM for HEK293 and human cells respectively).
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Chemical Structure - BML 280, PLD2 inhibitor (AB145226)
  • Chemical Structure

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Chemical Structure - BML 280, PLD2 inhibitor (AB145226)

2D chemical structure image of ab145226, BML 280, PLD2 inhibitor

Key facts

CAS number

1158347-73-9

Purity

>98%

Molecular weight

429.5 Da

Molecular formula

C<sub>2</sub><sub>5</sub>H<sub>2</sub><sub>7</sub>N<sub>5</sub>O<sub>2</sub>

PubChem

44138050

Nature

Synthetic

Solubility

Soluble in ethanol to 50 mM

Soluble in DMSO to 50 mM

Biochemical name

N-(2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)quinoline-3-carboxamide

Biological description

Potent, selective PLD2 inhibitor (IC50 values are 90 and 500 nM for HEK293 and human cells respectively).

Canonical smiles

C1CN(CCC12C(=O)NCN2C3=CC=CC=C3)CCNC(=O)C4=CC5=CC=CC=C5N=C4

InChi

InChI=1S/C25H27N5O2/c31-23(20-16-19-6-4-5-9-22(19)27-17-20)26-12-15-29-13-10-25(11-14-29)24(32)28-18-30(25)21-7-2-1-3-8-21/h1-9,16-17H,10-15,18H2,(H,26,31)(H,28,32)

InChiKey

WJOCDBUFEUKYNI-UHFFFAOYSA-N

IUPAC Name

N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl]quinoline-3-carboxamide

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Complementary Products

Biochemicals

AB145227

BML 279, PLD1 and PLD2 inhibitor

Chemical Structure - BML 279, PLD1 and PLD2 inhibitor (AB145227)

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Proteins & Peptides

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SDS-PAGE - Recombinant Human UBE2M/UBC12 protein (AB128447)

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Proteins & Peptides

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Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Store under desiccating conditions|The product can be stored for up to 12 months
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Supplementary information

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

Phospholipase D1 (PLD1) and Phospholipase D2 (PLD2) are enzymes that hydrolyze phosphatidylcholine to produce phosphatidic acid and choline. PLD1 and PLD2 are isoforms with significant roles in cellular functions. PLD1 has a molecular mass of approximately 120 kDa and is widely expressed in various tissues including the brain liver and heart. Alternate names for PLD1 include PLD1A and hPLD1. PLD2 similar in structure shares overlapping functions with PLD1. Both isoforms are localized in cellular membranes where they perform their enzymatic activity.
Biological function summary

PLD enzymes participate in signal transduction and membrane trafficking. PLD1 and PLD2 play roles in vesicle transport cytoskeletal organization and cellular proliferation. They are not typically part of large multiprotein complexes however they associate with other proteins like protein kinase C and small GTPases during signal transduction. By influencing intracellular pathways PLD1 and PLD2 contribute to diverse physiological processes.

Pathways

PLD1 and PLD2 are key players in the phosphatidylinositol signaling system and the mTOR pathway. Within the phosphatidylinositol signaling system PLD1 and PLD2 work with proteins like phosphatidylinositol 3-kinase (PI3K) helping regulate cell survival and growth. In the mTOR pathway which connects nutrient availability to cellular growth these enzymes interact with mTOR complexes affecting protein synthesis and autophagy.

PLD1 and PLD2 have implications in cancer and neurological disorders. In cancer upregulation of PLD enzymes associates with tumorigenesis and metastasis potentially through interactions with proteins like Ras and Rho GTPases. In neurological disorders aberrant PLD activity links to Alzheimer's disease where PLD enzymes may interact with amyloid precursor protein influencing amyloid-beta production. Understanding PLD1 and PLD2 functions offers insights into therapeutic strategies for these conditions.
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Product protocols

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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Cell biology international 43:678-694 PubMed30977575

2019

Role of PLD-PKCζ signaling axis in p47phox phosphorylation for activation of NADPH oxidase by angiotensin II in pulmonary artery smooth muscle cells.

Applications

Unspecified application

Species

Unspecified reactive species

Sajal Chakraborti,Jaganmay Sarkar,Tapati Chakraborti
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