KIN Human
Description
KIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
ENGFKCHCMS ESHQRQLLLA SENPQQFMDY FSEEFRNDFL ELLRRRFGTK RVHNNIVYNE YISHREHIHM NATQWETLTD FTKWLGREGL CKVDETPKGW YIQYIDRDPE TIRRQLELEK
KKKQDLDDEE KTAKFIEEQV RRGLEGKEQE VPTFTELSRE NDEEKVTFNL SKGACSSSGA
TSSKSSTLGP SALKTIGSSA SVKRKESSQS STQSKEKKKK KSALDEIMEI EEEKKRTART
DYWLQPEIIV KIITKKLGEK YHKKKAIVKE VIDKYTAVVK MIDSGDKLKL DQTHLETVIP
APGKRILVLN GGYRGNEGTL ESINEKTFSA TIVIETGPLK GRRVEGIQYE DISKLA.
Product Science Overview
The recombinant human KIN protein is typically produced in Escherichia coli (E. coli) and is often tagged with a His-tag at the N-terminus to facilitate purification. The protein corresponds to the amino acids 1-393 of the human KIN sequence . The theoretical molecular weight of the recombinant KIN protein is approximately 47.8 kDa, although the observed molecular weight may vary due to post-translational modifications and other experimental factors .
KIN17 is ubiquitously expressed in various tissues, with the highest levels found in muscle, heart, and testis . This protein is involved in binding to curved DNA and has been shown to interact with the Large T antigen in SV40-transformed fibroblasts, reducing T-antigen-dependent DNA replication . The overexpression of KIN17 in these fibroblasts suggests its potential role in regulating DNA replication and maintaining genomic stability.
Recombinant human KIN protein is widely used in research to study its role in DNA replication, repair, and transcription. Its ability to bind to DNA and RNA makes it a valuable tool for understanding the molecular mechanisms underlying these processes. Additionally, the recombinant form of KIN17 is used in various biochemical assays and structural studies to elucidate its function and interactions with other proteins and nucleic acids .
For optimal stability, the recombinant human KIN protein should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s integrity . The protein is typically supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.2 M NaCl, and 20% glycerol .
