Rabbit Anti-Jund Catalog No

Qty: 100μg/400 μL Rabbit anti-JunD Catalog No. 38-2900 Lot No. Rabbit anti-JunD

FORM This polyclonal antibody is supplied as a 400 µL aliquot at a concentration of 0.25 mg/mL in phosphate buffered saline (pH 7.4) containing 0.1% sodium azide. This antibody is epitope-affinity purified from rabbit antiserum.

PAD: ZMD.362

IMMUNOGEN Synthetic peptide derived from the C-terminal region of the human JunD protein.

SPECIFICITY This antibody reacts with the human and mouse JunD proteins. It recognizes both forms of JunD (full-length, JunD-FL, and truncated, Δ JunD). On Western blots, it identifies bands at ~35 kDa and ~40 kDa, representing the two forms of JunD. Bands of unknown origin may be observed in some lysates at ~100 kDa and ~150 kDa. Based on amino acid homology, reactivity with rat is expected.

REACTIVITY Reactivity has been confirmed with human HeLa, LNCaP, PC-3, U-2-OS, and mouse NIH 3T3 cell lysates.

Sample Western Immunoprecipitation Blotting (Native) Human +++ 0* Mouse +++ ND Rat ND ND (Excellent +++, Good++, Poor +, No reactivity 0, Not applicable N/A, Not Determined ND) *IP was not suitable with U-2-OS cell lysates under the conditions tested.

USAGE Working concentrations for specific applications should be determined by the investigator. Appropriate concentrations will be affected by several factors, including secondary antibody affinity, antigen concentration, sensitivity of detection method, temperature and length of incubations, etc. The suitability of this antibody for applications other than those listed below has not been determined. The following concentration ranges are recommended starting points for this product.

Western Blotting: 1-3 μg/mL

STORAGE Store at 2-8°C for up to one month. Store at –20°C for long-term storage. Avoid repeated freezing and thawing.

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BACKGROUND The JunD transcription factor is a basic region leucine zipper DNA-binding protein, and a member of the Jun family of proteins, which also includes c-Jun and JunB.1 Jun proteins can homodimerize or heterodimerize with other Jun family members, or heterodimerize with Fos family members (cFos, FosB, Fra-1, and Fra-2) to form the activator protein 1 transcription factor (AP-1).2-7 The various dimers differ in their ability to transactivate AP-1-dependent genes. Jun B8,9 and JunD1,10 are almost identical to c-Jun in their C-terminal regions, which are involved in dimerization and DNA binding, whereas their N-terminal domains, which are involved in transcriptional activation, diverge.

Two distinct forms of JunD, JunD full length (JunD-FL)(~40 kDa) and Δ JunD (~35 kDa), are ubiquitously expressed, and are generated by the use of two highly conserved translation start codons within a single JunD mRNA.11-13 The two forms of the protein differ only in a 48-amino acid N-terminal extension present in the mouse JunD full-length protein (43 amino acids in the human protein). 11-13 Both isoforms of JunD are phosphorylated by Jun N-terminal kinases (JNKs) at three identical residues, and both contain a docking domain that specifically binds JNKs, however, the two forms demonstrate differential responses to JNK signaling pathways.14

REFERENCES 1. Ryder K, et al. PNAS 86:1500-1503, 1989. 2. Angel P & Karin M. Biochim Biophys Acta 1072:129-157, 1991. 3. Hai TW, et al. Genes Dev 3:2083-2090, 1989. 4. Halazonetis TD, et al. Cell 55:917-924, 1988. 5. Nakabeppu Y, et al. Cell 55:907-915, 1988. 6. Smeal T, et al. Genes Dev 3:2091-2100, 1989. 7. van Dam H & Castellazzi M. Oncogene 20:2453-2464, 2001. 8. Ryder K & Nathans D. PNAS 85:8464-8467, 1988. 9. Castellazzi M, et al. PNAS 88:8890-8894, 1991. 10. Hirai S, et al. Embo J 8:1433-1439, 1989. 11. Lallemand D, et al. Oncogene 14:819-830, 1997. 12. Okazaki S, et al. Biochem Biophys Res Commun 250:347-353, 1998. 13. Yazgan O & Pfarr CM. Cancer Res 61:916-920, 2001. 14. Yazgan O & Pfarr CM. J Biol Chem 277:29710-29718, 2002.