unspecific bands on WB - extremely weak band at 72kDa but no change upon knockdown with siRNA
SAB1103260
Anti-DCAF15 (567-580) antibody produced in rabbit
IgG fraction of antiserum
Anti-DCAF15 (567-580) antibody produced in rabbit
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Synonym(s):
Anti-C19orf72, Anti-DDB1 and CUL4 associated factor 15
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200 μL
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~66 kDa
species reactivity
human
technique(s)
western blot: 1:500-1:2,000
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... DCAF15(90379)
1 of 4
This Item | SAB1100322 | HPA041575 | HPA044504 |
|---|---|---|---|
| antibody form IgG fraction of antiserum | antibody form IgG fraction of antiserum | antibody form affinity isolated antibody | antibody form affinity isolated antibody |
| conjugate unconjugated | conjugate unconjugated | conjugate unconjugated | conjugate unconjugated |
| Quality Level 200 | Quality Level 200 | Quality Level 100 | Quality Level 100 |
| biological source rabbit | biological source rabbit | biological source rabbit | biological source rabbit |
| mol wt antigen ~66 kDa | mol wt antigen ~21 kDa | mol wt - | mol wt - |
| clone polyclonal | clone polyclonal | clone polyclonal | clone polyclonal |
General description
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.
Immunogen
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.
Biochem/physiol Actions
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).
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.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
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)
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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