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DDX3 (DEAD Box Protein 3 X-chromosomal, DBX, Helicase-Like Protein 2, HLP2)

Cat no: D1660-22B


Supplier: United States Biological
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DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX3 interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. The DDX3 gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog. Alternative splicing of this gene generates 2 transcript variants, which are divergent in the 3' UTR. Applications: Suitable for use in Western Blot and Immunoprecipitation. Other applications not tested. Recommended Dilution: Western Blot: 1:1000-10.000 Immunoprecipitation: 2-5ug/ml Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Catalogue number: D1660-22B
Reactivities: Human
Hosts: Rabbit
Applications: Immunoprecipitation, Western Blot
Size: 100ul
Form: Supplied as a liquid in Tris-buffered saline, 0.1% BSA, 0.09% sodium azide.
P type: Pab
Isotype: IgG
Purity: Purified by immunoaffinity chromatography.
Alternative names: DDX 3, DDX-3, DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 3, DEAD Box Polypeptide, X-linked, CAP-Rf
Additional info: Recognizes human DDX3. Recognizes an epitope to a region between aa1-50 of human DEAD (Asp-Glu-Ala-Asp) box polypeptide 3.

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