DREF Monoclonal Antibody (OTI1F7), Invitrogen™
Manufacturer: Thermo Scientific
Select a Size
| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| Each of 1 | PIMA526035-Each-of-1 | In Stock | ₹ 52,198.50 |
PIMA526035 - Each of 1
In Stock
Quantity
1
Base Price: ₹ 52,198.50
GST (18%): ₹ 9,395.73
Total Price: ₹ 61,594.23
Antigen
DREF
Classification
Monoclonal
Concentration
1 mg/mL
Formulation
PBS with 1% BSA, 50% glycerol and 0.02% sodium azide; pH 7.3
Gene Accession No.
O96006
Gene Symbols
ZBED1
Immunogen
Full length human recombinant protein of ZBED1 produced in HEK293T cell
Quantity
100μL
Primary or Secondary
Primary
Target Species
Human
Product Type
Antibody
Isotype
IgG2a
Applications
Flow Cytometry, Immunohistochemistry (Paraffin), Western Blot
Clone
OTI1F7
Conjugate
Unconjugated
Gene
ZBED1
Gene Alias
Ac-like transposable element; ALTE; BED-type zinc finger domain-containing protein 1; DNA replication-related element binding factor; DREF; dREF homolog; hDREF; KIAA0785; Putative Ac-like transposable element; TRAMP; ZBED1; Zinc finger BED domain-containing protein 1; zinc finger BED-type containing 1; zinc finger, BED-type containing 1
Host Species
Mouse
Purification Method
Affinity Chromatography
Regulatory Status
RUO
Gene ID (Entrez)
9189
Content And Storage
-20° C, Avoid Freeze/Thaw Cycles
Form
Liquid
Related Products
Description
- ZBED1, also known as DREF, is the human homolog of the Drosophila protein DREF, a transcriptional regulatory factor required for expression of genes involved in DNA replication and cell proliferation
- RNA interference (RNAi) experiments targeting ZBED1 RNA resulted in the inhibition of S phase entry and reduction of histone H1 mRNA in HeLa cells, suggesting that ZBED1 also plays a role in cell proliferation in human cells
- At least 22 ribosomal proteins (RPs) possess ZBED1 binding sites in their promoters; anti-ZBED1 RNAi also resulted in decreased RP gene expression
- Immunoprecipitation analyses have shown that ZBED1 self-associates in vivo via a carboxyl-terminal hATC domain, and this self-association is required for nuclear localization and DNA binding.