This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This DHX9 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human DHX9.
DHX9
Reactivity: Human
ELISA, IHC
Host: Rabbit
Polyclonal
unconjugated
Application Notes
WB: 1:1000
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
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
4 °C,-20 °C
Expiry Date
6 months
Goshima, Kawamura, Fukumoto, Miura, Honma, Satoh, Wakamatsu, Yamamoto, Kimura, Nishikawa, Andoh, Iida, Ishikawa, Ito, Kagawa, Kaminaga, Kanehori, Kawakami, Kenmochi, Kimura, Kobayashi, Kuroita et al.: "Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. ..." in: Nature methods, Vol. 5, Issue 12, pp. 1011-7, (2008) (PubMed).
Zhang, Grosse: "Domain structure of human nuclear DNA helicase II (RNA helicase A)." in: The Journal of biological chemistry, Vol. 272, Issue 17, pp. 11487-94, (1997) (PubMed).
Abdelhaleem, Hameed, Klassen, Greenberg: "Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T cell granules and vesicles." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 156, Issue 6, pp. 2026-35, (1996) (PubMed).
Lee, Hurwitz: "Human RNA helicase A is homologous to the maleless protein of Drosophila." in: The Journal of biological chemistry, Vol. 268, Issue 22, pp. 16822-30, (1993) (PubMed).
Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alteration of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Component of the CRD-mediated complex that promotes MYC mRNA stability. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.