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Key Documents

AV49811

Sigma-Aldrich

Anti-LENG4 antibody produced in rabbit

IgG fraction of antiserum

Synonym(s):

Anti-BB1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

53 kDa

species reactivity

horse, dog, human, pig

concentration

0.5 mg - 1 mg/mL

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... LENG4(79143)

General description

Membrane bound O-acyltransferase domain containing 7 (MBOAT7; LENG4; LPLAT7) belongs to membrane-bound O-acyltransferase (MBOAT) family. The protein shows an endoplasmic reticulum-like reticular pattern and perinuclear staining in HEK293 cells.

Immunogen

Synthetic peptide directed towards the C terminal region of human LENG4

Application

Anti-LENG4 antibody produced in rabbit is suitable for western blotting at a concentration of 5.0μg/ml. The antibody has been used for western blotting for proteins isolated from mice brain tissue.

Biochem/physiol Actions

Membrane bound O-acyltransferase domain containing 7 (MBOAT7; LENG4) is an integral membrane protein important for reacylation of phospholipids. The reacylation is an important step in the recycling of phospholipids via the Land cycle. LENG4 is highly specific for arachidonoyl-coenzyme A and is involved in arachidonate recycling. LENG4 interacts with the small subunit of serine palmitoyltransferase a (ssSPTa). This interaction is important for LENG4-dependent incorporation of arachidonic acid into phosphatidylinositol.

Sequence

Synthetic peptide located within the following region: LSAYWHGLHPGYYLSFLTIPLCLAAEGRLESALRGRLSPGGQKAWDWVHW

Physical form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Miriam Longo et al.
Cellular and molecular gastroenterology and hepatology, 13(3), 759-788 (2021-11-26)
The I148M Patatin-like Phospholipase Domain-containing 3 (PNPLA3), the rs641738 in the Membrane bound O-acyltransferase domain containing 7-transmembrane channel-like 4 (MBOAT7-TMC4) locus, and the E167K Transmembrane 6 Superfamily Member 2 (TM6SF2) polymorphisms represent the main predisposing factors to nonalcoholic fatty liver disease
Karen E Anderson et al.
PloS one, 8(3), e58425-e58425 (2013-03-09)
We disrupted the gene encoding lysophosphatidylinositol-acyltransferase-1 (LPIAT1) in the mouse with the aim of understanding its role in determining cellular phosphoinositide content. LPIAT1(-/-) mice were born at lower than Mendelian ratios and exhibited a severe developmental brain defect. We compared
Yusuke Hirata et al.
Genes to cells : devoted to molecular & cellular mechanisms, 18(5), 397-409 (2013-03-21)
Lysophosphatidylinositol acyltransferase 1 (LPIAT1), also known as MBOAT7, is a phospholipid acyltransferase that selectively incorporates arachidonic acid (AA) into the sn-2 position of phosphatidylinositol (PI). We previously demonstrated that LPIAT1 regulates AA content in PI and plays a crucial role
Miguel A Gijón et al.
The Journal of biological chemistry, 283(44), 30235-30245 (2008-09-06)
The cycle of deacylation and reacylation of phospholipids plays a critical role in regulating availability of arachidonic acid for eicosanoid production. The major yeast lysophospholipid acyltransferase, Ale1p, is related to mammalian membrane-bound O-acyltransferase (MBOAT) proteins. We expressed four human MBOATs
Hideo Shindou et al.
Journal of lipid research, 50 Suppl, S46-S51 (2008-10-22)
Cells of all organisms are enclosed by a plasma membrane containing bipolar lipids, cholesterol, and proteins. Cellular membranes contain several classes of glycerophospholipids, which have numerous structural and functional roles in cells. Polyunsaturated fatty acids including arachidonic acid and eicosapentaenoic

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