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R5280

Sigma-Aldrich

Anti-phospho-RanGAP1 (pSer428) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Ran GTPase activating protein-1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~60 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

indirect immunofluorescence: 5-10 μg/mL using HeLa cells
western blot: 1.5-3.0 μg/mL using HEK-293T cell lysate expressing human RanGAP1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pSer428)

Gene Information

human ... RANGAP1(5905)

General description

The gene for Ran GTPase activating protein 1 (RANGAP1) is located on the human chromosome 22q13.2.

Specificity

Anti-phospho-RanGAP1 (pSer428) specifically recognizes human phospho-RanGAP1 (pSer428) (not yet tested in other species).

Application

Anti-phospho-RanGAP1 (pSer428) antibody produced in rabbit has been used in western blotting.

Biochem/physiol Actions

However, the SUMO-1 modification induces the interaction of RanGAP1 with the interphase nuclear pore complex (NPC) through binding to the nucleoporin Ras-related nuclear protein 1 binding protein 2 (RANBP2) and to Ubc9. RanGAP1 is phosphorylated on residues Thr409, Ser442 and Ser428. Phosphorylated RanGAP1 may aid the translocation of specific SUMO target proteins to RanBP2′s catalytic domain.
Ran GTPase Activating Protein 1 (RanGAP1) is a key regulator of Ran activity, by specifically inducing its GTPase activity. RanGAP1 is conjugated to the small ubiquitin-related modifier protein (SUMO-1). The activity of RanGAP1 is not substantially altered by SUMO-1 modification. Phosphorylation ensues before the breakdown of the nuclear envelope and is sustained during the entire mitosis process.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2–8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

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

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
Reverter D and Lima CD
Nature, 435(7042), 687-687 (2005)
Jomon Joseph et al.
Current biology : CB, 14(7), 611-617 (2004-04-06)
RanGAP1 is the activating protein for the Ran GTPase. Vertebrate RanGAP1 is conjugated to a small ubiquitin-like protein, SUMO-1. This modification promotes association of RanGAP1 with the interphase nuclear pore complex (NPC) through binding to the nucleoporin RanBP2, also known
Ran GTPase-activating protein 1 is a therapeutic target in diffuse large B-cell lymphoma
Chang K C, et al.
Testing, 8(11), e79863-e79863 (2013)
ON 01910. Na inhibits growth of diffuse large B-cell lymphoma by cytoplasmic sequestration of sumoylated C-MYB/TRAF6 complex
Dai YH, et al.
Translational Research, 175(11), 129-143 (2016)
Alexandre Amlie-Wolf et al.
Nucleic acids research, 46(17), 8740-8753 (2018-08-17)
The majority of variants identified by genome-wide association studies (GWAS) reside in the noncoding genome, affecting regulatory elements including transcriptional enhancers. However, characterizing their effects requires the integration of GWAS results with context-specific regulatory activity and linkage disequilibrium annotations to

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