Recombinant Human Cell Cycle Checkpoint Protein Rad1 (RAD1) Protein (GST)

Name: Recombinant Human Cell Cycle Checkpoint Protein Rad1 (RAD1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09138P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Cell Cycle Checkpoint Protein Rad1 (RAD1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O60671
Target Symbol	RAD1
Synonyms	Cell cycle checkpoint protein Hrad1 ; Cell cycle checkpoint protein Rad 1 A / B; Cell cycle checkpoint protein RAD1; Checkpoint control protein HRAD1; Checkpoint control protein RAD1; DNA repair exonuclease; DNA repair exonuclease rad1; DNA repair exonuclease rad1 homolog; DNA repair exonuclease REC1; DNA repair protein RAD1; EC 3.1.11.2; Exonuclease homolog RAD1; GTP-binding protein RAD; hRAD 1; hRAD1; MGC77779; RAD 1; RAD; RAD1; RAD1 homolog (S. pombe); RAD1 homolog; Rad1 like DNA damage checkpoint; Rad1 like DNA damage checkpoint protein; RAD1; S. pombe; homolog of; Rad1-like DNA damage checkpoint protein; RAD1_HUMAN; Ras associated with diabetes; REC 1; REC1; RRAD
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIKVTVENAKCVQANAFIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSPMPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLREAFSELDMTSEVLQITMSPDKPYFRLSTFGNAGSSHLDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPDEEVPESES
Expression Range	1-282aa
Protein Length	Full Length
Mol. Weight	58.8kDa
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. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity.
Subcellular Location	Nucleus.
Protein Families	Rad1 family
Database References	HGNC: 9806 OMIM: 603153 KEGG: hsa:5810 STRING: 9606.ENSP00000340879 UniGene: PMID: 26954070 Intramolecular binding of the rad9 C-terminus in the checkpoint clamp Rad9-Hus1-Rad1 is closely linked with its DNA binding. PMID: 26088138 Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies. PMID: 22586102 The RAD1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins. PMID: 21978893 CK2 plays a crucial role in the ATR-dependent checkpoint pathway through its ability to phosphorylate Ser-341 and Ser-387 of the Rad9 subunit of the Rad9-Hus1-Rad1 complex 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 Rad9, Hus1, and Rad1 heterotrimeric complex chromatin binding is a proximal event in the checkpoint signaling cascade PMID: 12228248 RAD1 is a potential intrinsic chaperone in the stabilization of HUS1 for the heterotrimeric (RAD9-RAD1-HUS1) checkpoint complex formation. PMID: 15122316 The human Rad9/Rad1/Hus1 complex interacts with and stimulates DNA polymerase beta activity. PMID: 15314187 complex with rad9 and hus1 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 hRad1 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; this association is mediated through direct interaction between Jab1 and Rad1, one of the subunits of the 9-1-1 complex PMID: 17583730 Human thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. PMID: 17855402 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

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.