Recombinant Human Trimethylguanosine Synthase (TGS1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-03151P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Trimethylguanosine Synthase (TGS1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-03151P
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Product Overview

Description Recombinant Human Trimethylguanosine Synthase (TGS1) 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 Q96RS0
Target Symbol TGS1
Synonyms Cap specific guanine N2 methyltransferase; Cap-specific guanine-N2 methyltransferase; CLL associated antigen KW 2; CLL-associated antigen KW-2; DKFZp762A163; FLJ22995; HCA137; Hepatocellular carcinoma associated antigen 137; Hepatocellular carcinoma-associated antigen 137; NCOA6IP; Nuclear receptor coactivator 6 interacting protein; Nuclear receptor coactivator 6-interacting protein; PIMT; PIPMT; PRIP interacting protein PIPMT; PRIP interacting protein with methyltransferase domain; PRIP interacting protein with methyltransferase motif; PRIP-interacting protein with methyltransferase motif; SEREX defined; TGS 1; Tgs1; TGS1_HUMAN; Trimethylguanosine synthase; Trimethylguanosine synthase homolog (S. cerevisiae); Trimethylguanosine synthase homolog
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVVFLSPPWGGPDYATAETFDIRTMMSPDGFEIFRLSKKITNNIVYFLPRNADIDQVASLAGPGGQVEIEQNFLNNKLKTITAYFGDLIRRPASET
Expression Range 713-853aa
Protein Length Partial
Mol. Weight 31.6kDa
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 Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation.
Subcellular Location Cytoplasm. Nucleus, Cajal body. Nucleus, nucleolus.
Protein Families Methyltransferase superfamily, Trimethylguanosine synthase family
Database References

HGNC: 17843

OMIM: 606461

KEGG: hsa:96764

STRING: 9606.ENSP00000260129

UniGene: PMID: 26738492

  • Self-association of Tgs1p and its catalytic activity were prerequisite to bypass the requirement for its accessory factor Swm2p for efficient pre-rRNA processing and snRNA trimethylation. PMID: 26074133
  • PIMT was identified as a key player responsible for glycated low density lipoproteins induced vascular endothelial cell apoptosis. PMID: 23922881
  • isoforms of the PIMT/Tgs1 protein with an RNA methyltransferase domain function both in the nucleus and in the cytoplasm PMID: 12943661
  • The protein L-isoaspartyl (D-aspartyl) methyltransferase (PIMT) is an enzyme that recognizes and repairs the abnormal L-isoaspartyl residues in proteins. PMID: 21204776
  • The structure-function data highlight a strictly essential pi-cation interaction between Trp766 and the m(7)G base and a network of important enzymic contacts to the cap triphosphate via Lys646, Tyr771, Arg807, and Lys836. PMID: 20360394
  • Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation. PMID: 11912212
  • proteasome maturation constitutes a mechanism regulating Tgs1 function by generating Tgs1 species with different substrate specificities, subcellular localizations, and functions. PMID: 18039666
  • These results highlight that PIMT expression is regulated by ROS and could primarily act as an antioxidant enzyme. PMID: 18407833
  • present a biochemical characterization of the human Tgs1 guanine-N2 methyltransferase reaction and identify individual amino acids required for methyltransferase activity in vitro and in vivo PMID: 18775984
  • m(7)GpppA binds via its adenosine moiety to the structurally conserved adenosylmethionine-binding pocket. The m(7) guanosine is unbound. The crystallized TGS1 fragment is catalytically inactive, but a fragment that is 17 AAs longer exhibits activity. PMID: 19307714
  • The crystal structure of the substrate bound methyltransferase domain as well as mutagenesis studies provide insight into the catalytic mechanism of TGS1. PMID: 19386620

    • 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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