Antibodies to Proteins in the
SMC Complexes
February 2010
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Overview
Structural maintenance of chromosomes (SMC) proteins are critical regulators of chromosome organization and function (1). This family of chromosomal ATPases is highly conserved from bacteria and archaeal species to vertebrates. There are at least six eukaryotic SMC proteins. The SMC proteins display a common primary architecture that consists of five structural domains. The five domains include two nucleotide-binding motifs termed the Walker A and Walker B motifs located at the N- and C-terminus, a central “hinge” domain, and two coiled-coil motifs that flank the central “hinge”. The SMC proteins associate in specific dimer pairs and arrange in an anti-parallel, two-armed structure that folds into a V-shape at the “hinge” domain. Three SMC complexes have been identified and are defined by the SMC subunits which associate to form a heterodimer and their respective associated proteins. SMC1 and SMC3 are part of the cohesin holocomplex which also includes at least two non-SMC subunits Scc1/mcd1/rad21 and scc3/SAs. The cohesin complex is required for holding together sister chromatids after replication in S-phase and throughout G2 phase. SMC2 and SMC4 are part of the condensin complex which also includes three non-SMC subunits: CAP-D2, CAP-G, and CAP-H. Condensin plays a critical role in mitotic chromosome condensation during prophase and metaphase and segregation of sister chromatids during anaphase. SMC5 and SMC6 are part of a not-yet-named octameric complex (2). The function of this complex is not fully understood; but it appears to be polyfunctional. The SMC5/SMC6 complex displays activities similar to cohesin and condensin, and it appears to be mainly involved in a variety of DNA repair pathways, replication, and recombination. The necessity of SMC proteins to the chromosome cycle has been well demonstrated, and more studies of these factors are needed for a better understanding of the complex dynamics of chromosome structure and function. |
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 Detection of Human CAP-G by WB and IP . Sample: Whole cell lysate from HeLa (5, 15 and 50 mcg for WB; 1 mg for IP, 20% of IP loaded) and 293T (50 mcg for WB) cells. Antibodies: Affinity purified rabbit anti-CAP-G antibody A300-602A used for WB at 0.04 mcg/ml (A) and 1 mcg/ml (B) and for IP at 3 mcg/mg lysate (B). CAP-G was also immunoprecipitated using rabbit anti-CAP-G antibody BL2935, which binds an upstream epitope. For detecting immunoprecipitated CAP-G, ReliaBLOT Reagents and Procedures (Cat. No. WB120) were used. Detection: Chemiluminescence with exposure times of 30 seconds (A and B). |
 Detection of Human CAP-D3 by WB and IP. Samples: Whole cell lysate from HeLa (5, 15 and 50 mcg for WB; 1 mg for IP, 20% of IP loaded) and 293T (50 mcg for WB) cells. Antibodies: Affinity purified rabbit anti-CAP-D3 antibody A300-604A used for WB at 0.04 mcg/ml (A) and 1 mcg/ml (B) and for IP at 3 mcg/mg lysate (B). CAP-D3 was also immunoprecipitated using rabbit anti-CAP-D3 antibody BL2943, which binds an upstream epitope. For detecting immunoprecipitated CAP-D3, ReliaBLOT Reagents and Procedures (Cat. No. WB120) were used. Detection: Chemiluminescence with exposure times of 10 seconds (A) and 3 seconds (B). |
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Bethyl Laboratories' portfolio of polyclonal antibodies commercially available includes over 3500 polyclonal antibodies to over 1300 proteins. We test our antibodies in a wide range of applications including ELISA, western blot, immunoprecipitation, immunohistochemistry, and immunocytochemistry. We have recently validated many of our antibodies for flow cytometry and ChIP. Our antibody range also includes secondary antibodies, loading controls and antibodies to epitope tags. |
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