DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 20 (DDX20) (AA 667-783) antibody

Details for Product No. ABIN968759
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Synonyms DDX20, DP103, GEMIN3, dp103, Dp103, si:dkey-193l3.3, wu:fb16g08, wu:fb59a11
AA 667-783
(17), (14), (8), (4), (3), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
(55), (13), (4)
(45), (12)
Clonality (Clone)
Monoclonal ()
(2), (2), (2), (2), (2), (2)
Western Blotting (WB)
(53), (36), (12), (11), (8), (3), (3), (3), (2), (2)
Pubmed 4 references available
Quantity 50 μg
Shipping to United States (Change)
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Catalog No. ABIN968759
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Immunogen Human DP103
Clone 2
Isotype IgG2b
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name DP103/Gemin3
Background DEAD box proteins, a family of putative RNA helicases, are characterized by eight conserved amino acid motifs that are arranged in a core region as found in the prototypical member of the family, eIF-4A. The family's name is derived from the amino acid sequence Asp-Glu-Ala-Asp (DEAD) that is located within the ATP hydrolysis motif. DEAD box proteins have been implicated in translation initiation and RNA splicing, degradation, and stability. The DEAD box protein, DP103, contains seven N-terminal helicase motifs characteristic of DEAD box proteins followed by an SMN interaction domain (SID). DP103 mRNA has been reported to be widely expressed, and DP103 protein is found in the nucleus and cytoplasm. SMN, the gene mutated in spinal muscular atrophy, forms a 20S nuclear complex that includes DP103, SIP1 (SMN-interacting protein 1), and snRNPs. DP103 also co-localizes with SMN and SIP1 to nuclear bodies called gems. In addition, DP103 interacts with the proximal repressor domain of steroidogenic factor-1, a nuclear receptor essential for development of the gonads, adrenal gland, and hypothalamic nuclei. Thus, DP103 may have roles in SMN complex modulation of RNA splicing and in transcriptional repression. This antibody is routinely tested by western blot analysis.
Synonyms: Gemin3, DEAD box Protein-103, Ddx20
Molecular Weight 103 kDa

Related Products: ABIN968537, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 20 (DDX20) (AA 667-783) antibody Western blot analysis of DP103 on a Jurkat cell lysate (Human T-cell leukemia, ATCC TIB-152). Lane 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of the mouse anti-human DP103 antibody.
Product cited in: Ou, Mouillet, Yan et al.: "The DEAD box protein DP103 is a regulator of steroidogenic factor-1." in: Molecular endocrinology (Baltimore, Md.), Vol. 15, Issue 1, pp. 69-79, 2001 (PubMed).

Meister, Bühler, Laggerbauer et al.: "Characterization of a nuclear 20S complex containing the survival of motor neurons (SMN) protein and a specific subset of spliceosomal Sm proteins." in: Human molecular genetics, Vol. 9, Issue 13, pp. 1977-86, 2000 (PubMed).

Charroux, Pellizzoni, Perkinson et al.: "Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems." in: The Journal of cell biology, Vol. 147, Issue 6, pp. 1181-94, 2000 (PubMed).

Grundhoff, Kremmer, Türeci et al.: "Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C." in: The Journal of biological chemistry, Vol. 274, Issue 27, pp. 19136-44, 1999 (PubMed).

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