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Mouse Anti-MBOAT7 Recombinant Antibody (1D4) (CBMAB-A4922-LY)

The product is antibody recognizes LENG4. The antibody 1D4 immunoassay techniques such as: sELISA, ELISA.
See all MBOAT7 antibodies
Published Data
Fig.1 Co‐immunoprecipitation of EGFP‐ssSPTa with LPIAT1‐myc.
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Fig.2 Small subunit of serine palmitoyltransferase a (ssSPTa) colocalizes with lysophosphatidylinositol acyltransferase 1 (LPIAT1) in HEK293 cells.
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Fig.3 Human MBOAT proteins were analyzed by immunoblotting with an anti-V5 antibody.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
1D4
Antibody Isotype
IgG2a, κ
Application
sELISA, ELISA

Basic Information

Immunogen
LENG4 (NP_077274.2, 96 a.a. ~ 192 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Concentration
0.5 mg/mL
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
MEMBRANE BOUND O-ACYLTRANSFERASE DOMAIN CONTAINING 7
Introduction
This gene encodes a member of the membrane-bound O-acyltransferases family of integral membrane proteins that have acyltransferase activity. The encoded protein is a lysophosphatidylinositol acyltransferase that has specificity for arachidonoyl-CoA as an acyl donor. This protein is involved in the reacylation of phospholipids as part of the phospholipid remodeling pathway known as the Land cycle. Alternative splicing results in multiple transcript variants. [provided by RefSeq]
Entrez Gene ID
79143
UniProt ID
Q96N66
Alternative Names
BB1; LENG4; LPIAT; hMBOA-7
Function
Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) leading to the production of a phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle (PubMed:18772128, PubMed:18094042).

Prefers arachidonoyl-CoA as the acyl donor, thus contributing to the regulation of free levels arachidonic acid in cell (PubMed:18772128, PubMed:18094042).

In liver, participates in the regulation of triglyceride metabolism through the phosphatidylinositol acyl-chain remodeling regulation (PubMed:32253259).
Biological Process
Layer formation in cerebral cortex Source: UniProtKB
Lipid modification Source: GO_Central
Phosphatidylcholine acyl-chain remodeling Source: UniProtKB
Phosphatidylinositol acyl-chain remodeling Source: UniProtKB
Phosphatidylinositol biosynthetic process Source: UniProtKB
Regulation of triglyceride metabolic process Source: UniProtKB
Ventricular system development Source: Ensembl
Cellular Location
Endoplasmic reticulum membrane
Note: Localized in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria.
Involvement in disease
Intellectual developmental disorder, autosomal recessive 57 (MRT57):
A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT57 patients have moderate to severe intellectual disability, and delayed psychomotor development with poor or absent speech. Some patients manifest seizures and autistic features.
Topology
Cytoplasmic: 1-5
Helical: 6-22
Lumenal: 23-33
Helical: 34-57
Cytoplasmic: 58-73
Helical: 74-93
Lumenal: 94-194
Helical: 195-212
Cytoplasmic: 213-231
Helical: 232-261
Lumenal: 262-426
Helical: 427-447
Cytoplasmic: 448-472

Caddeo, A., Spagnuolo, R., & Maurotti, S. (2023). MBOAT7 in liver and extrahepatic diseases. Liver International, 43(11), 2351-2364.

Wang, K., Lee, C. W., Sui, X., Kim, S., Wang, S., Higgs, A. B., ... & Farese Jr, R. V. (2023). The structure of phosphatidylinositol remodeling MBOAT7 reveals its catalytic mechanism and enables inhibitor identification. Nature Communications, 14(1), 3533.

Varadharajan, V., Massey, W. J., & Brown, J. M. (2022). Membrane-bound O-acyltransferase 7 (MBOAT7)-driven phosphatidylinositol remodeling in advanced liver disease. Journal of Lipid Research, 63(7).

Xia, M., Chandrasekaran, P., Rong, S., Fu, X., & Mitsche, M. A. (2021). Hepatic deletion of Mboat7 (LPIAT1) causes activation of SREBP-1c and fatty liver. Journal of lipid research, 62.

Caddeo, A., Hedfalk, K., Romeo, S., & Pingitore, P. (2021). LPIAT1/MBOAT7 contains a catalytic dyad transferring polyunsaturated fatty acids to lysophosphatidylinositol. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1866(5), 158891.

Tanaka, Y., Shimanaka, Y., Caddeo, A., Kubo, T., Mao, Y., Kubota, T., ... & Kono, N. (2021). LPIAT1/MBOAT7 depletion increases triglyceride synthesis fueled by high phosphatidylinositol turnover. Gut, 70(1), 180-193.

Meroni, M., Dongiovanni, P., Longo, M., Carli, F., Baselli, G., Rametta, R., ... & Valenti, L. (2020). Mboat7 down-regulation by hyper-insulinemia induces fat accumulation in hepatocytes. EBioMedicine, 52.

Meroni, M., Longo, M., Fracanzani, A. L., & Dongiovanni, P. (2020). MBOAT7 down-regulation by genetic and environmental factors predisposes to MAFLD. EBioMedicine, 57.

Helsley, R. N., Varadharajan, V., Brown, A. L., Gromovsky, A. D., Schugar, R. C., Ramachandiran, I., ... & Brown, J. M. (2019). Obesity-linked suppression of membrane-bound O-acyltransferase 7 (MBOAT7) drives non-alcoholic fatty liver disease. Elife, 8, e49882.

Caddeo, A., Jamialahmadi, O., Solinas, G., Pujia, A., Mancina, R. M., Pingitore, P., & Romeo, S. (2019). MBOAT7 is anchored to endomembranes by six transmembrane domains. Journal of Structural Biology, 206(3), 349-360.

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For research use only. Not intended for any clinical use.

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