Technical Data
C7853-05C
Connexin 32
Description:
Intercellular communication through gap junctions plays an important role in a variety of cellular processes including homeostasis, morphogenesis, cell differentiation and growth control (1-4). Gap junctions are transmembrane channels that serve to directly link neighboring cells by mediating the exchange of low-molecular weight (< 1200D) metabolites, ions and second messengers. Gap junctions are formed by the interaction of hemichannels (connexons) on adjacent cells. The connexon itself is composed of a hexameric assembly of Connexin proteins. Connexins are highly homologous proteins encoded by a multigene family. The connections exhibit similar structural features which include a cytoplasmic amino terminal region, four transmembrane domains, two extracellular loops, and a carboxy-terminal cytoplasmic tail of varying length. Comparison of the amino acid sequences of the various Connexin family members indicate that the two areas of greatest divergence amongst the Connexin family members are the intracellular loop connecting the second and third transmembrane segments and the carboxy-terminal tail (1,2). These domains are, therefore, thought to mediate Connexin-type speci c properties including phosphorylation, responses to gating stimuli, as well as assembly and membrane turnover. Modulation of gap junction communication can be achieved by multiple mechanisms and can occur very rapidly or over a period of several hours. These mechanisms include alterations in transcription, translation, stability, postranslational processing (especially phosphorylation), gating, and insertion or removal from the plasma membrane. Interestingly, reduction or alterations in the levels or types of Connexin expressed in a given cell type has been found to correlate with tumor progression and metastasis (5). Connexin 30 (Cx-30) is a recently identi ed 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% amino acid sequence identity) (6,7). The two show distinct tissue expression patterns: Cx30 is highly expressed in adult skin and brain but not in embryonic and fetal brain (6,7). Cx26 is expressed highly in prenatal brain, decreasing after birth.

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

Recommended Dilution:
ELISA: 0.1-1.0ug/ml
Western Blot (8,10): 0.5ug/ml. Detects a 32kD protein in rat liver preparations enriched for integral membrane proteins. Note: samples were not boiled prior to running SDS-PAGE.
Immunohistochemistry (Frozen sections: 8,11): 1-2ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
50ug4C (-20C Glycerol)Blue IceRatRabbit
Concentration:
~0.125mg/ml
Immunogen:
Synthetic peptide corresponding to a portion of the cytoplasmic loop of rat connexin 32.
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in PBS, pH 7.4, 0.1% sodium azide, before the addition of glycerol to 40%.
Specificity:
Reacts predominantly with rat Connexin 32. Crossreactive bands may be detected in the 50-65kD range. These bands may represent Connexin 32 dimers, but this has not been con rmed. Species Crossreactivity: human and mouse.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Kumar, M., Gilula, M.B., Cell 84: 381-388 (1996). 2. Saez, J.C., et al., In Advances in Second Messenger and Phosphoprotein Research. eds S., Shenolikar and A., Narin. Raven Press, New York (1993). 3. Bennet, M.V.L., et al., Neuron 6: 305-320 (1990). 4. Kuraoka, A., et al., J. Histochem. and Cytochem. 41: 971-980 (1993). 5. Wilgenbus, KK., et al., Int. J. Cancer 51: 522-529 (1992). 6. Dahl, E. et al., J. Biol. Chem. 271: 17903-17910 (1996). 7. Nagy, J.I., et al., Neuroscience 78: 533-548 (1997). 8. Rash, JE, et al., J. Neuroscience 21(6): 1983-2000 (2001). (Also used for freeze-fracture immunogold labeling, double labeling, and electron microscopy.) 9. Rash, JE, et al., PNAS 97(13): 7573-7578 (2000). 10. Nusrat, A., et al., J. Biol. Chem. 275(38): 29816-29822 (2000). 11. Weglarz, TC, et al., PNAS 97(23): 12595-12600 (2000).