Technical Data
Connexin 26 (CX26, Gap Junction Beta 2 Protein, CXB-2)
Connexin 30 (Cx-30) is a recently identified member of the connexin gene family, isolated by screening a mouse genomic library with a rat Cx26 probe (6). Cx30 is closely related to Cx26 (77% aa sequence identity) (7,8) but the two show distinct tissue expression patterns: Cx30 is highly expressed in adult skin and brain while but not in embryonic and fetal brain (7,8). On the other hand, Cx26 is expressed highly in prenatal brain, decreasing after birth.

Suitable for use in ELISA, Western Blot, Immunohistochemistry and Immunofluorescence. Other applications not tested.

Recommended Dilutions:
ELISA: 0.1-1.0 mg/ml
Western Blot: 0.5ug/ml. A 26kD protein from mouse liver membrane, mouse brain extract and rat brain extract was detected (samples were not boiled prior to running SDS-PAGE). A few crossreactive bands were detected in the 45-50kD range. The identity of these proteins has yet to be con rmed; however, it is possible these bands represent dimeric forms of the Connexin 26 protein.
Immunohistochemistry (Frozen): 10ug/ml. Staining of frozen sections of human cochlea showed positive reactivity for Connexin 26.
Optimal dilutions to be determined by the researcher.

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. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
50ug-20CBlue IceRatRabbit
Peptide corresponding to a portion of the cytoplasmic loop of rat connexin 26.
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, pH 7.4, 0.09% sodium azide.
Recognizes rat Connexin 26. Species Crossreactivity: mouse and human.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Kelsell DP, et al. Nature 387:80-83 (1997). 2. Kumar, M. and Gilula, M.B., Cell 84:381:388 (1996). 3. Saez, J.C., et al; In Advances in Second Messenger and Phosphoprotein Research; eds S., Shenolikar and A., Narin. Raven Press, New York (1993). 4. Bennet, M.V.L., et al; Neuron 6:305-320 (1990). 5. Kuraoka, A., et al; J. Histochem. and Cytochem. 41:971-980 (1993). 6. Wilgenbus, KK., et al; Int. J. Cancer 51:522-529 (1992). 7. Dahl, E. et al., J. Biol. Chem. 271:17903-17910 (1996). 8. Nagy, J.I., et al., Neuroscience 78:533-548 (1997). 9. Nagy, J.I., et al; Neuroscience 88(2):447-468 (1999). 10. Hosny S. and Jennes L.; Neuroendocrinology 67:101-108 (1998). 11. Bittman, K.S. et al; Cerebral Cortex 9:188-195 (1999).