Revision 1

#48243Store at -20C

1 Kit

(7 x 20 microliters)

Cell Signaling Technology

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For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
NKX2.5 (E1Y8H) Rabbit mAb 8792 20 µl 30-42 kDa Rabbit IgG
GATA-6 (D61E4) XP® Rabbit mAb 5851 20 µl 55 kDa Rabbit IgG
MEF2C (D80C1) XP® Rabbit mAb 5030 20 µl 50-60 kDa Rabbit IgG
α-Actinin (D6F6) XP® Rabbit mAb 6487 20 µl 100 kDa Rabbit IgG
Troponin I (D6F8) Rabbit mAb 13083 20 µl 28 kDa Rabbit IgG
Troponin T (Cardiac) Antibody 5593 20 µl 40 kDa Rabbit 
Connexin 43 Antibody 3512 20 µl 39, 41, 43, 44 kDa Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 

Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.

Description

The Cardiogenesis Marker Antibody Sampler Kit provides an economical means of evaluating proteins involved in heart development. This kit contains enough antibody to perform two western blot experiments per primary antibody.

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Background

Cardiogenesis is a complex developmental event involving numerous transcription factors. NKX2.5 is a member of the NKX homeobox transcription factor family, which plays an essential role in heart development and is among the earliest factors expressed in the cardiac lineage in developing embryos. Mutations in NKX2.5 are associated with several congenital heart conditions, such as atrial defect with atrioventricular conduction defects (ASD-AVCD) and Tetralogy of Fallot (TOF) (1,2). GATA proteins comprise a group of transcription factors that are related by the presence of conserved zinc finger DNA binding domains, which bind directly to the nucleotide sequence core element GATA (3-5). GATA-6 plays a critical role in endoderm development and knock out of GATA-6 is embryonic lethal due to defects in formation of the heart tube and a failure to develop extraembryonic endoderm (6). MEF2C is a member of the MEF2 (myocyte enhancer factor 2) family of transcription factors. The MEF2 family members were originally described as muscle-specific DNA binding proteins that recognize MEF2 motifs found within the promoters of many muscle-specific genes (7,8). α-Actinin was first recognized as an actin cross-linking protein. The α-actinin protein interacts with a large number of proteins involved in signaling to the cytoskeleton, including those involved in cellular adhesion, migration, and immune cell targeting (9). The muscle isoforms 2 and 3 (ACTN2, ACTN3) localize to the Z-discs of striated muscle and to dense bodies and plaques in smooth muscle (9). Troponin, working in conjunction with tropomyosin, functions as a molecular switch that regulates muscle contraction in response to changes in the intracellular Ca2+ concentration. Troponin consists of three subunits: the Ca2+-binding subunit troponin C (TnC), the tropomyosin-binding subunit troponin T (TnT), and the inhibitory subunit troponin I (TnI) (10). Assays for measuring serum concentrations of cardiac muscle TnT (cTNT), as well as cTnI, have been reported for analyzing cardiac injury. Connexin 43 (Cx43) is a member of the large family of gap junction proteins, which assemble as a hexamer and are transported to the plasma membrane to create a hemichannel that can associate with hemichannels on nearby cells to create cell-to-cell channels. Gap junction communication is important in development and regulation of cell growth. Phosphorylation of Cx43 is important in regulating assembly and function of gap junctions (11,12).

  1. Benson, D.W. et al. (1999) J Clin Invest 104, 1567-73.
  2. Reamon-Buettner, S.M. and Borlak, J. (2010) Hum Mutat 31, 1185-94.
  3. Ko, L.J. and Engel, J.D. (1993) Mol Cell Biol 13, 4011-22.
  4. Merika, M. and Orkin, S.H. (1993) Mol Cell Biol 13, 3999-4010.
  5. Lowry, J.A. and Atchley, W.R. (2000) J Mol Evol 50, 103-15.
  6. Cai, K.Q. et al. (2008) Dev Dyn 237, 2820-9.
  7. Martin, J.F. et al. (1994) Mol Cell Biol 14, 1647-56.
  8. Yu, Y.T. et al. (1992) Genes Dev 6, 1783-98.
  9. Otey, C.A. and Carpen, O. (2004) Cell Motil Cytoskeleton 58, 104-11.
  10. Ward, D.G. et al. (2002) J Biol Chem 277, 41795-801.
  11. Musil, L.S. et al. (1990) J Cell Biol 111, 2077-88.
  12. Musil, L.S. and Goodenough, D.A. (1991) J Cell Biol 115, 1357-74.

Background References

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