Recombinant Human Checkpoint Protein Hus1 (HUS1) Protein (His-SUMO)

Name: Recombinant Human Checkpoint Protein Hus1 (HUS1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09994P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Checkpoint Protein Hus1 (HUS1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O60921
Target Symbol	HUS1
Synonyms	Checkpoint protein HUS1; hHUS1; HUS1 (S. pombe) checkpoint homolog; Hus1; HUS1 checkpoint homolog (S. pombe); HUS1 Checkpoint Protein; HUS1 protein; HUS1+ - like protein; HUS1_HUMAN; Hydroxyurea-sensitive 1, S. pombe, homolog of
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	KFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSMWCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS
Expression Range	2-280aa
Protein Length	Partial
Mol. Weight	47.6kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Nucleus. Cytoplasm, cytosol.
Protein Families	HUS1 family
Database References	HGNC: 5309 OMIM: 603760 KEGG: hsa:3364 STRING: 9606.ENSP00000258774 UniGene: Hs.152983
Tissue Specificity	Ubiquitous.

Gene Functions References

These results suggest that p21(Waf1/CIP1) and Hus1 play crucial roles in the generation and transmission of bystander damage signals after low-dose alpha-particle irradiation. PMID: 26600172
adenine glycosylase activity, mismatch recognition properties and interaction with protein partners of MUTYH and 5 MAP variants were examined; P502L and R520Q had reduced affinity for PCNA; only Q324H was found to have reduced affinity for Hus1 PMID: 26377631
Intramolecular binding of the rad9 C-terminus in the checkpoint clamp Rad9-Hus1-Rad1 is closely linked with its DNA binding. PMID: 26088138
these pockets were not required for 9-1-1 chromatin localization or ATR-mediated CHK1 activation but were necessary for interactions between HUS1 and its binding partner MYH PMID: 25911100
Expression of cell cycle regulatory factors hus1, gadd45a, rb1, cdkn2a and mre11a correlates with expression of clock gene per2 in human colorectal carcinoma tissue. PMID: 24062075
HUS1 polymorphisms act as risk breast cancer modifiers in the group of non-carriers of BRCA1/2 mutations. PMID: 22926736
Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies. PMID: 22586102
The HUS1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins. PMID: 21978893
The HUS1 protein interacts with casein kinase 2. PMID: 20545769
9-1-1 complex is a component of the mismatch repair involved in MNNG-induced damage response. PMID: 20188637
Rad9-Rad1-Hus1 complex enhances in vitro activity of 8-oxoguanine DNA glycosylase. PMID: 19615952
downregulation by specific antisense oligonucleotides sensitizes human lung carcinoma cells to treatment with the DNA-damaging agent cisplatin PMID: 11920544
Rad9, Hus1, and Rad1 heterotrimeric complex chromatin binding is a proximal event in the checkpoint signaling cascade PMID: 12228248
HUS1 is an unstable protein that is actively degraded via the ubiquitin-proteasome pathway. Its expression can be stabilized by treating cells with proteasome-specific inhibitors. PMID: 15122316
The human Rad9/Rad1/Hus1 complex interacts with and stimulates DNA polymerase beta activity. PMID: 15314187
complex with rad1 and rad9 is a damage-specific activator of flap endonuclease 1 PMID: 15556996
The long-patch base excision machinery is an important target of the Rad9-Rad1-Hus1 complex, thus enhancing the quality control of DNA. PMID: 15871698
PCNA and the Rad9/Rad1/Hus1 complex can independently bind and activate Fen1; acetylation of Fen1 by p300-HAT abolished the stimulatory effect of the complex but not that of PCNA, suggesting a possible mechanism of regulation of this repair pathway PMID: 16216273
human DNA ligase I is stimulated by the Rad9-rad1-Hus1 checkpoint complex PMID: 16731526
These data provide in vivo evidence that the human 9-1-1 complex participates in DNA repair in addition to its previously described role in DNA damage sensing. PMID: 16814252
Human NEIL1 DNA glycosylase activity is significantly stimulated by Hus1 and by the Rad9/Rad1/Hus1 heterotrimer. PMID: 17395641
we report successful tri-cistronic cloning, overexpression and purification of a three-protein complex of Rad9, Rad1 and Hus1 using a single hexa-histidine tag. PMID: 17493829
Jab1 physically associates with the 9-1-1 complex (Rad1-Rad9-Hus1) PMID: 17583730
Human thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. PMID: 17855402
Hus1 levels correlated significantly with the clinicopathologic factors of bad prognosis in epithelial ovarian tumors PMID: 18156970
Loss of HUS1 sensitizes cells to etopside-induced apoptosis by regulating BH3-only proteins. PMID: 18794804
The DNA binding domain (DBD) within the hLigI catalytic fragment interacts with both PCNA and the heterotrimeric cell-cycle checkpoint clamp, hRad9-hRad1-hHus1 (9-1-1). PMID: 19523882
The interdomain connecting loops (IDC loop) of hRad9, hHus1, and hRad1 are largely divergent and unique structural features of the 9-1-1 complex that are proposed to contribute to DNA damage recognition. PMID: 19535328
Functional study of the yeast homolog. PMID: 9524127

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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