DDAH I (C-19): Sc-26068

DDAH I (C-19): Sc-26068

SANTA CRUZ BIOTECHNOLOGY, INC. DDAH I (C-19): sc-26068 The Power to Question BACKGROUND APPLICATIONS DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl DDAH I (C-19) is recommended for detection of DDAH I of mouse, rat and arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric human origin by Western Blotting (starting dilution 1:200, dilution range oxide synthases, and may be involved in in vivo modulation of nitric oxide 1:100-1:1000) and immunofluorescence (starting dilution 1:50, dilution production. Impairment of DDAH causes ADMA accumulation and a reduc- range 1:50-1:500). tion in cGMP generation. DDAH II, the predominant DDAH isoform in endothelial cells, facilitates the induction of nitric oxide synthesis by all- RECOMMENDED SECONDARY REAGENTS trans-Retinoic acid (atRA). DDAH proteins are highly expressed in colon, kid- To ensure optimal results, the following support (secondary) reagents are ney, stomach and liver tissues. recommended: 1) Western Blotting: use donkey anti-goat IgG-HRP: sc-2020 (dilution range: 1:2000-1:100,000) or Cruz Marker™ compatible donkey anti- REFERENCES goat IgG-HRP: sc-2033 (dilution range: 1:2000-1:5000), Cruz Marker™ 1. Nakagomi, S., et al. 1999. Dimethylarginine dimethylaminohydrolase Molecular Weight Standards: sc-2035, TBS Blotto A Blocking Reagent: (DDAH) as a nerve-injury-associated molecule: mRNA localization in the sc-2333 and Western Blotting Luminol Reagent: sc-2048. 2) Immunofluores- rat brain and its coincident up-regulation with neuronal NO synthase cence: use donkey anti-goat IgG-FITC: sc-2024 (dilution range: 1:100-1:400) (nNOS) in axotomized motoneurons. Eur. J. Neurosci. 11: 2160-2166. or donkey anti-goat IgG-TR: sc-2783 (dilution range: 1:100-1:400) with PMID 10336684 UltraCruz™ Mounting Medium: sc-24941. 2. Knipp, M., et al. 2001. Structural and functional characterization of the Zn(II) site in dimethylargininase-1 (DDAH-1) from bovine brain. Zn(II) RESEARCH USE release activates DDAH-1. J. Biol. Chem. 276: 40449-40456. For research use only, not for use in diagnostic procedures. PMID 11546769 PROTOCOLS 3. Leiper, J., et al. 2002. S-nitrosylation of dimethylarginine dimethylamino- hydrolase regulates enzyme activity: further interactions betwen nitric See our web site at www.scbt.com or our catalog for detailed protocols oxide synthase and dimethylarginine dimethylaminohydrolase. Proc. Natl. and support products. Acad. Sci USA 99: 13527-13532. 4. Lin, K.Y., et al. 2002. Impaired nitric oxide synthase pathway in diabetes mellitus: role of asymmetric dimethylarginine and dimethylaminohydro- lase. Circulation 106: 987-992. 5. Achan, V., et al. 2002. All-trans-retinoic acid increases nitric oxide synth- esis by endothelial cells: a role for the induction of dimethylaminohydro- lase. Circ. Res. 90: 764-769. 6. Knipp, M., et al. 2003. Zn(II)-free dimethylargininase-1 (DDAH-1) is inhibit- ed upon specific Cys-S-nitrosylation. J. Biol. Chem. 278: 3410-3416. PMID 12441345 7. Swiss-Prot/TrEMBL (O94760). World Wide Web URL: http://www.expasy. ch/sprot/sprot-top.html SOURCE DDAH I (C-19) is an affinity purified goat polyclonal antibody raised against a peptide mapping within an internal region of DDAH I of human origin. PRODUCT Each vial contains 200 µg IgG in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin. Blocking peptide available for competition studies, sc-26068 P, (100 µg pep- tide in 0.5 ml PBS containing < 0.1% sodium azide and 0.2% BSA). STORAGE Store at 4° C, **DO NOT FREEZE**. Stable for one year from the date of shipment. Non-hazardous. No MSDS required. Santa Cruz Biotechnology, Inc. 1.800.457.3801 831.457.3800 fax 831.457.3801 Europe +00800 4573 8000 49 6221 4503 0 www.scbt.com.

View Full Text

Details

  • File Type
    pdf
  • Upload Time
    -
  • Content Languages
    English
  • Upload User
    Anonymous/Not logged-in
  • File Pages
    1 Page
  • File Size
    -

Download

Channel Download Status
Express Download Enable

Copyright

We respect the copyrights and intellectual property rights of all users. All uploaded documents are either original works of the uploader or authorized works of the rightful owners.

  • Not to be reproduced or distributed without explicit permission.
  • Not used for commercial purposes outside of approved use cases.
  • Not used to infringe on the rights of the original creators.
  • If you believe any content infringes your copyright, please contact us immediately.

Support

For help with questions, suggestions, or problems, please contact us