Technical Data
DnaJ (HSP40, HDJ 2) (BSA & Azide Free)
Novel human homolog of E. colis DnaJ protein from heat shock protein 40 family. HSP40 is involved in chaperonic protein folding. HDJ 2 is cytoplasmic and nuclear membrane associated protein; upon heat shock it migrates and becomes associated with the Golgi complex, nucleolus and nuclear membrane. HDJ 2 has a prenylated C-terminus and is not inducible upon heat shock.

Suitable for use in Immunofluorescence, Flow Cytometry, Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot: 0.5-1ug/ml for 2 hours ar RT.
Immunoprecipitation (Native and denatured): 2ug/mg protein lysate. Use Protein G.
Immunohistochemistry (Formalin/paraffin): 1-2ug/ml for 30 minutes at RT. Staining of formalin-fixed tissues requires boiling tissue sections in 10mM citrate buffer, pH 6.0, for 10-20 minutes followed by cooling at RT for 20 minutes.
Optimal dilutions to be determined by the researcher.

Positive Control:
MAD109, Raji cells, Tonsil

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
MabIgG13F200Affinity Purified
100ul-20CBlue IceHumanMouse
Recombinant fragment corresponding to aa1-179 at the N-terminal of HDJ-2 fusion protein. MW of Antigen: 44-47kD. Cellular Localization: Cytoplasm (ground state) and Golgi complex, nucleolus, and nuclear membrane (upon heat shock).
Purified by Protein G affinity chromatography.
Supplied as a liquid in 10mM PBS, pH 7.4. Also available with BSA and azide. See D4015-09A.
Recognizes human HDJ 2 (DnaJ). No crossreactivity with HDJ 1. Associates with a 53kD protein of unknown identity. Species Crossreactivity: monkey, porcine, rabbit, mouse, rat, hamster and bacteria.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Sugito, K., et al., Febs Letters 358(2): 161164 (1995). 2. Frydman, J., et al., Nature 370(6485): 111117 (1994). 3. Ohta, T., et al., Journal of Bacteriology 176(15): 47794783 (1994). 4. Chellaiah, A., et al., Biochimica et Biophysica Acta, 1174(1): 111-113 (1993). 5. Hattori, H., et al., Journal of Cell Science 104(3): 629638 (1993). 6. Ohtsuka, K., Biochemical and Biophysical Research Communication 197(1): 235240 (1993). 7. Hattori, H., et al., Cell Structure and Function 17(1): 7786 (1992).