HuS1 recombinant protein

HuS1, 1-280aa, Human, His tag, E Coli

Cat. Num. AAA203967

• Gene Names: HUS1; hHUS1
• Applications: SDS-Page
• Purity: > 95% by SDS-PAGE
• Synonyms: HuS1; 1-280aa; Human; His tag; E Coli; checkpoint protein HuS1; HuS1 recombinant protein

• Host: E Coli
• Purity/Purification: > 95% by SDS-PAGE
• Form/Format: Liquid. In 20 mM Tris-HCl Buffer (pH 8.0) containing 100 mM NaCl, 40% glycerol
• Concentration: 0.25mg/ml (determined by Bradford assay) (varies by lot)
• Sequence: MGSSHHHHHH SSGLVPRGSH MKFRAKIVDG ACLNHFTRIS NMIAKLAKTC TLRISPDKLN FILCDKLANG GVSMWCELEQ ENFFNEFQME GVSAENNEIY LELTSENLSR ALKTAQNARA LKIKLTNKHF PCLTVSVELL SMSSSSRIVT HDIPIKVIPR KLWKDLQEPV VPDPDVSIYL PVLKTMKSVV EKMKNISNHL VIEANLDGEL NLKIETELVC VTTHFKDLGN PPLASESTHE DRNVEHMAEV HIDIRKLLQF LAGQQVNPTK ALCNIVNNKM VHFDLLHEDV SLQYFIPALS
• Sequence Length: 280

• Applicable Applications for HuS1 recombinant protein: SDS-PAGE
• Antigen Species: Human
• Tag Information: His-tag
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for HuS1 recombinant protein

HuS1 is a component of an evolutionarily conserved, genotoxin-activated checkpoint complex. This protein associates with Rad9 and Rad1 to form the 9-1-1 (RAD9-RAD1-HuS1) complex, which localizes to DNA lesions and promotes DNA damage signaling and repair or apoptosis, cell cycle arrest. The trimeric complex is structurally similar to the proliferating cell nuclear antigen (PCNA) sliding clamp and interacts with Rad17 as a clamp-clamp loader pair during the DNA damage response. Recombinant human HuS1 protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography.

Product Categories/Family for HuS1 recombinant protein

Cell Cycle

References

Weiss RS., et al (2009) Proc Natl Acad Sci u S A. 106 (50):21282-7.; Roos-Mattjus P., et al (2002) J Biol Chem. 15;277 (46):43809-12.

NCBI and Uniprot Product Information

• NCBI GI #: 4758576
• NCBI GeneID: 3364
• NCBI Accession #: NP_004498
• NCBI GenBank Nucleotide #: NM_004507.3
• UniProt Accession #: O60921; B4DFI9
• Molecular Weight: 33.8 kDa (300aa), confirmed by MALDI-TOF
• NCBI Official Full Name: checkpoint protein HUS1
• NCBI Official Synonym Full Names: HUS1 checkpoint clamp component
• NCBI Official Symbol: HUS1
• NCBI Official Synonym Symbols: hHUS1
• NCBI Protein Information: checkpoint protein HUS1
• UniProt Protein Name: Checkpoint protein HUS1
• Protein Family: Checkpoint protein
• UniProt Gene Name: HUS1
• UniProt Synonym Gene Names: hHUS1

NCBI Description

The protein encoded by this gene is a component of an evolutionarily conserved, genotoxin-activated checkpoint complex that is involved in the cell cycle arrest in response to DNA damage. This protein forms a heterotrimeric complex with checkpoint proteins RAD9 and RAD1. In response to DNA damage, the trimeric complex interacts with another protein complex consisting of checkpoint protein RAD17 and four small subunits of the replication factor C (RFC), which loads the combined complex onto the chromatin. The DNA damage induced chromatin binding has been shown to depend on the activation of the checkpoint kinase ATM, and is thought to be an early checkpoint signaling event. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2011]

Uniprot Description

Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase.