HUS1 checkpoint protein is a part of the Hus1-Rad1-Rad9 heterotrimeric complex and forms a PCNA-ring-like structure. The HUS1 gene is mapped on the human chromosome at 7p12.3.
synthetic peptide corresponding to amino acids 253-269 of human Hus1, conjugated to KLH via an N-terminal cysteine residue.
Application
Anti-HUS1, C-terminal antibody produced in rabbit may be used in immunoblotting.
Biochem/physiol Actions
HUS1 protein along with cell cycle checkpoint proteins Rad1 and Rad9 is involved in cell cycle arrest as a response to DNA damage and acts as a sliding clamp. Upregulation of HUS1 gene expression leads to inhibition of cell proliferation, migration, invasion, and cell cycle arrest in hepatocellular carcinoma (HCC).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
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Unless otherwise stated in our catalog, our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Hus1, Rad1, and Rad9 are three evolutionarily conserved proteins required for checkpoint control in fission yeast. These proteins are known to form a stable complex in vivo. Recently, computational studies have predicted structural similarity between the individual proteins of Hus1-Rad1-Rad9
The HUS1 checkpoint clamp component (HUS1), which is a member of an evolutionarily conserved, genotoxin-activated checkpoint complex (Rad9-Rad1-Hus1 [9-1-1] complex), is involved in cell cycle arrest and DNA repair in response to DNA damage. We conducted this study to investigate
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