Skip to Content
Merck
CN
All Photos(4)

Key Documents

Safety Information

SAB4200645

Sigma-Aldrich

Monoclonal Anti-RNF4 antibody produced in mouse

clone RN.4, purified from hybridoma cell culture

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352203

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

RN.4, monoclonal

form

buffered aqueous solution

species reactivity

human

packaging

antibody small pack of 25 μL

concentration

~1 mg/mL

technique(s)

flow cytometry: 1-3 μg/test using HeLa cells
immunoblotting: 2-4 μg/mL using whole extracts of HEK-293 cells.
immunofluorescence: 0.25-0.5 μg/mL using HeLa cells.

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... RNF4(6047)

General description

RNF4 (ring finger protein 4), initially identified as a transcriptional cofactor, is an E3 ubiquitin ligase. As this protein contains both the SUMO-interacting motif (SIM) and RING finger domains, it links sumoylation to ubiquitination.

Immunogen

synthetic peptide corresponding to a sequence at the C terminal region of human RNF4

Biochem/physiol Actions

RNF4 (ring finger protein 4) plays a wide variety of physiological roles, such as targeting of proteins for degradation, including promyelocytic leukemia protein (PML), CENP-I (centromere protein I), hypoxia-inducible factor (HIF), PARP-1 (poly [ADP-ribose] polymerase 1) etc. It also induces the base excision repair machinery, thus controlling DNA methylation. It is involved in DNA demethylation therefore, promoting gene transcription. RNF4 acts upon the oncogenic protein, Tax, of human T-cell leukemia virus type 1 (HTLV-1), and it regulates its nucleo-cytoplasmic localization. Arsenic trioxide (ATO) facilitates the sumoylation of promyelocytic leukemia (PML) bodies, thus, increasing their RNF4-mediated SUMO-dependent ubiquitylation and degradation. RNF4 functions as a co-regulator of androgen receptor-dependent transcription and is expressed in mice testis. Therefore, it might be involved in spermatid maturation.

Physical form

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

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Expression of the nuclear RING finger protein SNURF/RNF4 during rat testis development suggests a role in spermatid maturation.
Yan W et al
Mechanisms of Development, 118(1-2), 247-253 (2002)
RING finger protein 4 (RNF4) derepresses gene expression from DNA methylation.
Wang Y
The Journal of Biological Chemistry, 289 (49), 33808-33813 (2014)
The Sumo-targeted ubiquitin ligase RNF4 regulates the localization and function of the HTLV-1 oncoprotein Tax.
Fryrear KA et al
Blood, 119(5), 1173-1181 (2012)
Stefan R Weisshaar et al.
FEBS letters, 582(21-22), 3174-3178 (2008-08-19)
We have recently reported that poly-SUMO-2/3 conjugates are subject to a ubiquitin-dependent proteolytic control in human cells. Here we show that arsenic trioxide (ATO) increases SUMO-2/3 modification of promyelocytic leukemia (PML) leading to its subsequent ubiquitylation in vivo. The SUMO-binding

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service