Product nameSMC1A peptide
See all SMC1A proteins and peptides
Our Abpromise guarantee covers the use of ab209494 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Blocking - Blocking peptide for Anti-SMC1A antibody [EPFHCR37F] (ab133643)
This is the blocking peptide for ab133643
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
- If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -20°C.
- Chromosome segregation protein SmcB
FunctionInvolved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.
Involvement in diseaseDefects in SMC1A are the cause of Cornelia de Lange syndrome type 2 (CDLS2) [MIM:300590]; also known as Cornelia de Lange syndrome X-linked. CDLS is a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. CDLS is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation and various other malformations including gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies.
Sequence similaritiesBelongs to the SMC family. SMC1 subfamily.
DomainThe flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 protein, forming a ring structure.
modificationsPhosphorylated by ATM upon ionizing radiation in a NBS1-dependent manner. Phosphorylated by ATR upon DNA methylation in a MSH2/MSH6-dependent manner. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation.
Cellular localizationNucleus. Chromosome. Chromosome > centromere > kinetochore. Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function. Integral component of the functional centromere-kinetochore complex at the kinetochore region during mitosis.
- Information by UniProt
ab209494 has not yet been referenced specifically in any publications.