Recombinant Human Dna Ligase 1 (LIG1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-10875P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Dna Ligase 1 (LIG1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-10875P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Dna Ligase 1 (LIG1) 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 P18858
Target Symbol LIG1
Synonyms DNA ligase 1; DNA ligase I; DNLI1_HUMAN; LIG 1; lig1; Ligase I DNA ATP dependent; MGC117397; MGC130025; Polydeoxyribonucleotide synthase [ATP] 1
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIEEVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSASTAKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPLKPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAFDLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCEGLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLLASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSAVWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQSQIQNQQGEDSGSDPEDTY
Expression Range 1-919aa
Protein Length Full Length
Mol. Weight 128.7kDa
Research Area Cell Cycle
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 DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Subcellular Location Nucleus.
Protein Families ATP-dependent DNA ligase family
Database References

Gene Functions References

  1. single-stranded break repair by human DNA ligase III isoforms reveal biochemical differences from DNA ligase PMID: 28751376
  2. A histone H3K9-like mimic within LIG1 is methylated by G9a and GLP and avidly binds UHRF1. Interaction with methylated LIG1 promotes the recruitment of UHRF1 to DNA replication sites and is required for DNA methylation maintenance. PMID: 28803780
  3. The rs156641 polymorphism of DNA ligase 1 (LIG1) was significantly associated with lung cancer risk, whereas no association was found between rs3730931/rs439132/rs20579 polymorphisms and lung cancer. PMID: 27352326
  4. Data suggest that DNA ligase I (LigI)-deficient 46BR.1G1 cells represent a model to investigate the biological effects of sub-lethal levels of DNA insults. PMID: 26151554
  5. The LIG1 CC genotype was associated with susceptibility to non-small cell lung cancer, and the AA genotype demonstrated increased radiosensitivity compared to the AC and CC genotypes. PMID: 26125914
  6. A novel method for monitoring functional lesion-specific recruitment of repair proteins in live cells. PMID: 25879709
  7. Ppolymorphisms in LIG1 affect its expression and may therefore change its function. PMID: 25189241
  8. there is no association between LIGI polymorphisms and cervical cancer risk. However, they may be playing an important role in modulating the risk of cervical adenocarcinoma in North Indian women PMID: 24084463
  9. DNA ligase I also interacts with replication factor C, the factor that loads the PCNA trimeric ring onto DNA. PMID: 22918593
  10. Data indicate that Ku70/Ku80 facilitates the cooperative binding of multiple XRCC4/Ligase IV (XL) and XLF molecules to DNA. PMID: 23620595
  11. Single nucleotide polymorphisms in LIG1 are associated with myelodysplastic syndromes. PMID: 23339595
  12. phosphorylation of serine 51 on hLigI plays a critical role in regulating the interaction between hLigI and RFC, which is required for efficient DNA replication and repair. PMID: 22952233
  13. Data show that association of study-wide significance (P < 8.2 x 10(-5)) was identified for single-nucleotide polymorphisms (SNP) in TP53, LIG1, and BIK. PMID: 22139380
  14. Kinetic mechanism of human DNA ligase I reveals magnesium-dependent changes in the rate-limiting step that compromise ligation efficiency. PMID: 21561855
  15. RNA silencing of human DNA ligase I expression severely reduced replication of viral DNA in cells infected with vaccinia virus ligase-deficient mutants. PMID: 20006844
  16. DNA ligase I competes with FEN1 to expand repetitive DNA sequences in vitro. PMID: 11948189
  17. stimulated by APE1 for progression through the base excision repair pathway PMID: 12200445
  18. phosphorylation of DNA ligase I and possibly other replicative enzymes is part of the mechanism that directs the disassembly of the replication machinery at the completion of S-phase. PMID: 12851383
  19. majority of single-strand DNA interruptions produced during the repair of alkylated DNA bases are repaired by the pathway mediated by Pol beta and either Lig I or Lig III PMID: 14627836
  20. crystal structure of human DNA ligase I (residues 233 to 919) in complex with a nicked, 5' adenylated DNA intermediate PMID: 15565146
  21. The human checkpoint sensor and alternative clamp Rad9-Rad1-Hus1 can interact with and specifically stimulate DNA ligase I PMID: 15871698
  22. LIG1-deficiency reduces recombinational repair of DNA double-strand beaks. PMID: 15907772
  23. human DNA ligase I is stimulated by the Rad9-rad1-Hus1 checkpoint complex PMID: 16731526
  24. siRNA mediated down-regulation of DNA ligase I in human HTD114 cells led to impaired end joining that was mediated by 2-, 3- or 10-bp microhomology. PMID: 18440984
  25. The LIG1 SNP 5'UTR showed a significant association with glioma risk. PMID: 19124499
  26. drastically reduced replicative LigI activity in 46BR.1G1 cells results in the accumulation of both single-stranded and double-stranded DNA breaks. PMID: 19223467
  27. a mutant version of hLigI, which mimics the hyperphosphorylated M-phase form of hLigI, does not interact with and is not inhibited by RFC, demonstrating that inhibition of ligation is dependent upon the interaction between hLigI and RFC PMID: 19223468
  28. 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
  29. Data support the notion that DNA ligase I participates in homology dependent pathways that deal with replication-associated lesions generated when replication fork encounters DNA damage. PMID: 19597347
  30. Data show that disruption of LigI and PCNA interactions influences trinucleotide repeat instability. PMID: 19628465

FAQs

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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.

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