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Key Documents

R0155

Sigma-Aldrich

Anti-Anti-RanGAP1 (C-terminal) antibody produced in rabbit

enhanced validation

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-Ran-GTPase-Activating Protein 1

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~65 kDa

Espèces réactives

human

Validation améliorée

recombinant expression
Learn more about Antibody Enhanced Validation

Concentration

~1 mg/mL

Technique(s)

indirect immunofluorescence: 5-10 μg/mL using HeLa cells
indirect immunofluorescence: suitable
western blot: 1-2 μg/mL using HEK-293T cells transfected with human RanGAP1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... RANGAP1(5905)
mouse ... Rangap1(19387)

Description générale

The unmodified form of RanGAP1 (65 kDa) is exclusively cytoplasmic, whereas the 90 kDa SUMO-1-modified form is associated with the cytoplasmic fibers of the nuclear pore complex (NPC).

Immunogène

synthetic peptide corresponding to amino acids 573-587 located at the C-terminus of human RanGAP1. The sequence is highly conserved (80% identity) in mouse RanGAP1.

Application

Anti-RanGAP1 (C-terminal) antibody produced in rabbit has been used for immunoblotting and listeriolysin O (LLO) purification.
Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.

Actions biochimiques/physiologiques

RanGAP1 (Ran GTPase Activating Protein 1, 65 kDa) is a key regulator of Ran activity, specifically inducing the GTPase activity of Ran. RanGAP1 is conjugated to the small ubiquitin-related modifier protein SUMO-1. The association of RanGAP1 with RanBP2 facilitates nuclear transport.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM 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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Listeria monocytogenes impairs SUMOylation for efficient infection
Ribet D, et al.
Nature, 464(7292), 1192-1192 (2010)
The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
Joseph J, et al.
Current Biology, 14(7), 611-617 (2004)
David Ribet et al.
Nature, 464(7292), 1192-1195 (2010-04-24)
During infection, pathogenic bacteria manipulate the host cell in various ways to allow their own replication, propagation and escape from host immune responses. Post-translational modifications are unique mechanisms that allow cells to rapidly, locally and specifically modify activity or interactions
Smriti Verma et al.
Molecular and cellular biology, 35(17), 2932-2946 (2015-06-24)
Posttranslational modifications (PTMs) can alter many fundamental properties of a protein. One or combinations of them have been known to regulate the dynamics of many cellular pathways and consequently regulate all vital processes. Understandably, pathogens have evolved sophisticated strategies to

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