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Key Documents

SAB1103260

Sigma-Aldrich

Anti-DCAF15 (567-580) antibody produced in rabbit

IgG fraction of antiserum

Synonyme(s) :

Anti-C19orf72, Anti-DDB1 and CUL4 associated factor 15

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~66 kDa

Espèces réactives

human

Technique(s)

western blot: 1:500-1:2,000

Numéro d'accès UniProt

Q66K64

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... DCAF15(90379)

Description générale

DCAF15 (DNA damage binding protein1 (DDB1) and cullin4 (CUL4) associated factor 15) gene in human chromosome, is mapped to 19p13.12. DCAF15 lacks protein interaction domain.
DCAF15 protein is a substrate receptor for E3 ligase. This protein is a part of the cullin 4-RING (CRL4)-DCAF15 E3 ubiquitin ligase.

Immunogène

synthetic peptide corresponding to amino acids 567-580 of human DCAF15

Application

Anti-DCAF15 (567-580) antibody produced in rabbit has been used in western blotting.

Actions biochimiques/physiologiques

DCAF15 (DNA damage binding protein 1 (DDB1) and cullin4 (CUL4) associated factor 15) is the vertebrate ortholog of Saccharomyces pombe chromosome licensing and DNA replication factor 2 (Cdt2) and is required for destruction of Cdt1 during S phase and after DNA damage in human cells.
DCAF15 protein plays a role in RNA splicing and cell apoptosis of various cancer cell lines. This protein is also involved in ubiquitination and degradation of splicing factor RNA binding motif protein 39 (RBM39).

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

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)

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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Consulter la Bibliothèque de documents

Expanding the spectrum of rearrangements involving chromosome 19: A mild phenotype associated with a 19p13.12-p13. 13 deletion
Marangi G, et al.
American Journal of Medical Genetics. Part A, 158(4), 888-893 (2012)
A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1
Jin J, et al.
Molecular Cell, 23(5), 709-721 (2006)
Zhi Chen et al.
Scientific reports, 7(1), 1175-1175 (2017-04-28)
Cell cycle progression in mammals is strictly controlled by a number of cyclin-dependent kinases (CDKs) and CDK inhibitors (CKIs), the expression of which is often dysregulated in cancer cells. Our previous work revealed that Cullin 4B (CUL4B), a critical component
Xiao Dong et al.
Aging, 13(7), 10603-10618 (2021-04-10)
Epithelial-mesenchymal transition (EMT) is an evolutionarily conserved developmental program that has been implicated in tumorigenesis and confers metastatic properties upon cancer cells. ZEB1 is a master transcription factor that activates the EMT process in various cancers. ZEB1 is reportedly degraded
Tabitha C Ting et al.
Cell reports, 29(6), 1499-1510 (2019-11-07)
Indisulam and related sulfonamides recruit the splicing factor RBM39 to the CRL4-DCAF15 E3 ubiquitin ligase, resulting in RBM39 ubiquitination and degradation. Here, we used a combination of domain mapping and random mutagenesis to identify domains or residues that are necessary

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