This antibody was purified using protein G column chromatography from culture supernatant of hybridoma cultured in a medium containing bovine IgG depleted (approximately 95%) fetal bovine serum and was filtered through a 0.22µm membrane.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Dot: Use at an assay dependent dilution.
WB: Use at an assay dependent dilution. Detects a band of approximately 32 kDa (predicted molecular weight of full length protein: 45 kDa).
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro.
Ubiquitously expressed in all tissues examined, with highest levels in skeletal muscle, heart and testis. Differentially expressed in non-tumorigenic and tumorigenic cell lines. Highly expressed in proliferating epithelial keratinocyte cells in vitro (at protein level).
Belongs to the KIN17 family. Contains 1 C2H2-type zinc finger.
The C-terminal domain (268-393) is organized into 2 subdomains that bear structural similarities to SH3-like domains. Both subdomains adopt a similar 5-stranded beta-barrel-like fold and are connected to each other by a short linker of 5 residues. The 5 beta-sheets are packed at approximately right angles against each other. A highly conserved groove formed at the interface between the 2 subdomains, comprised of Lys residues 302 and 391 and other positively charged residues, may possibly be the site of RNA-binding.
Nucleus. Cytoplasm. During S phase, strongly associated with the nuclear matrix, and to chromosomal DNA in the presence of DNA damage. Also shows cytoplasmic localization in elongated spermatids.