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Key Documents

SAB3500302

Sigma-Aldrich

Anti-LIS1 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-Lissencephaly 1, Anti-PAFAH, Anti-Platelet-activating factor acetylhydrolase

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
ID de substance PubChem :
Nomenclature NACRES :
NA.43

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

human, rat, mouse

Technique(s)

immunocytochemistry: suitable
immunofluorescence: suitable
indirect ELISA: suitable
western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

InChI

1S/C21H39O7P/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-21(23)27-18-20(22)19-28-29(24,25)26/h6-7,9-10,20,22H,2-5,8,11-19H2,1H3,(H2,24,25,26)/b7-6+,10-9+

Clé InChI

ZQTAMPRZFOOEEP-AVQMFFATSA-N

Informations sur le gène

human ... PAFAH1B1(5048)

Description générale

The gene PAFAH1B1 (platelet activating factor acetylhydrolase 1b regulatory subunit 1) encodes a protein named LIS1 (lissencephaly-1) that forms the α subunit of the intracellular Ib isoform of platelet-activating factor acteylhydrolase (PAFAH). The gene is mapped to human chromosome 17p13.3.

Immunogène

LIS1 antibody was raised against a 14 amino acid peptide from near the carboxy terminus of human LIS1.

Application

Monoclonal Anti-LIS1 antibody produced in mouse has been used in immunofluorescence.

Actions biochimiques/physiologiques

The heterotrimeric enzyme, platelet-activating factor acteylhydrolase (PAFAH), catalyzes the cleavage of acetyl group at the SN-2 position of platelet-activating factor. The α subunit encoded by the gene PAFAH1B1 (platelet activating factor acetylhydrolase 1b regulatory subunit 1) interacts with tubulin and affects microtubule dynamics. Mutations in this gene have been linked to Miller–Dieker lissencephaly, a human brain malformation characterized by a smooth cerebral surface and a disordered organization of the cortical layers resulting from a defect in neuronal migration.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Liaison

The action of this antibody can be blocked using blocking peptide SBP3500302.

Forme physique

Supplied in PBS with 0.02% sodium azide.

Clause de non-responsabilité

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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Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Isolation of a Miller-Dieker lissencephaly gene containing G protein beta-subunit-like repeats.
Reiner O
Nature, 364, 717-721 (1993)
Joseph M Villarin et al.
Nature communications, 7, 13865-13865 (2016-12-22)
Cytoplasmic dynein mediates retrograde transport in axons, but it is unknown how its transport characteristics are regulated to meet acutely changing demands. We find that stimulus-induced retrograde transport of different cargos requires the local synthesis of different dynein cofactors. Nerve
T Sapir et al.
The EMBO journal, 16(23), 6977-6984 (1998-01-31)
Forming the structure of the human brain involves extensive neuronal migration, a process dependent on cytoskeletal rearrangement. Neuronal migration is believed to be disrupted in patients exhibiting the developmental brain malformation lissencephaly. Previous studies have shown that LIS1, the defective

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