Rabbit anti-Human SMC3 Polyclonal Antibody

Uniprot Id

Q9UQE7

Target Species

Human

Target Name

SMC3

Target Full Name

Structural maintenance of chromosomes protein 3

Target Function

Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form 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. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement.

Target Involvement

Cornelia de Lange syndrome 3 (CDLS3)

Target Subcellular Location

Nucleus. Chromosome. Chromosome, centromere.

Target Protein Families

SMC family, SMC3 subfamily

Target Synonyms

BAM; Bamacan; Basement membrane associated chondroitin proteoglycan; Basement membrane-associated chondroitin proteoglycan; BMH; CDLS3; chondroitin sulfate proteoglycan 6 (bamacan); Chondroitin sulfate proteoglycan 6; Chromosome associated polypeptide; Chromosome-associated polypeptide; CSPG 6; CSPG6; hCAP; Human chromosome associated polypeptide; im:7142991; SMC 3; SMC protein 3; SMC-3; smc3; SMC3_HUMAN; SMC3L1; Structural maintenance of chromosome 3; Structural maintenance of chromosomes 3; Structural maintenance of chromosomes protein 3; u:fb22e01; wu:fc30d07

Target Background

This gene belongs to the SMC3 subfamily of SMC proteins. The encoded protein occurs in certain cell types as either an intracellular, nuclear protein or a secreted protein. The nuclear form, known as structural maintenance of chromosomes 3, is a component of the multimeric cohesin complex that holds together sister chromatids during mitosis, enabling proper chromosome segregation. Post-translational modification of the encoded protein by the addition of chondroitin sulfate chains gives rise to the secreted proteoglycan bamacan, an abundant basement membrane protein.