KIN (KIN. antigenic determinant of recA protein homolog (mouse))

Polyclonal antibody produced in rabbits immunized with a synthetic peptide corresponding to a region of human KIN.

Suggested starting concentrations are provided. Optimal dilutions should be determined by end-user. Differences in calculated versus apparent molecular weight may be due to post-translational modifications or protein hydrophobicity. Kin is a nuclear protein that forms intranuclear foci during proliferation and is redistributed in the nucleoplasm during the cell cycle. Short-wave ultraviolet light provokes the relocalization of the protein. suggesting its participation in the cellular

Interacts with SV40 large T antigen. Associated with DNA polymerase alpha RFC1 and cyclin A in multiprotein DNA replication complexes. Also associates with replication origins at the G1/S phase boundary and throughout the S phase in vivo.

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).

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.

Contains 1 C2H2-type zinc finger. Summary: The protein encoded by this gene is a nuclear protein that forms intranuclear foci during proliferation and is redistributed in the nucleoplasm during the cell cycle. Short-wave ultraviolet light provokes the relocalization of the protein suggesting its participation in the cellular response to DNA damage. Originally selected based on protein-binding with RecA antibodies the mouse protein presents a limited similarity with a functional domain of the bacterial RecA protein a characteristic shared by this human ortholog. Despras. E. . et al. . (2003) Radiat. Res. 159(6). 748-758.