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マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-Flag タグ

データシートレビュー関連製品プロトコル
Mouse GLRX cDNA クローン製品情報
Gene_bank_ref_id:NM_053108.4
cDNA サイズ:324bp
cDNA の説明:Full length Clone DNA of Mus musculus glutaredoxin with N terminal Flag tag.
遺伝子の別名:Grx1, Glrx1, TTase, C86710, D13Wsu156e
:Mouse
ベクター:pCMV3-N-FLAG
Plasmid:
制限サイト:
タグ シーケンス:FLAG Tag Sequence: GATTACAAGGATGACGACGATAAG
シーケンスの説明:
Sequencing primers:T7(TAATACGACTCACTATAGGG) BGH(TAGAAGGCACAGTCGAGG)
Promoter:Enhanced CMV mammalian cell promoter
Application:Stable or Transient mammalian expression
Antibiotic in E.coli:Kanamycin
Antibiotic in mammalian cell:Hygromycin
Shipping_carrier:Each tube contains lyophilized plasmid.
保存:The lyophilized plasmid can be stored at room temperature for three months.
FLAG Tag Info

FLAG-tag, or FLAG octapeptide, is a polypeptide protein tag that can be added to a protein using recombinant DNA technology. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild-type protein expressed by the host organism. It can also be used in the isolation of protein complexes with multiple subunits.

A FLAG-tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a FLAG-tag to this protein allows one to follow the protein with an antibody against the FLAG sequence. Examples are cellular localization studies by immunofluorescence or detection by SDS PAGE protein electrophoresis.

The peptide sequence of the FLAG-tag from the N-terminus to the C-terminus is: DYKDDDDK (1012 Da). It can be used in conjunction with other affinity tags, for example a polyhistidine tag (His-tag), HA-tag or Myc-tag. It can be fused to the C-terminus or the N-terminus of a protein. Some commercially available antibodies (e.g., M1/4E11) recognize the epitope only when it is present at the N-terminus. However, other available antibodies (e.g., M2) are position-insensitive.

マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-Flag タグ on other vectors
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, C-GFPSpark タグMG52947-ACGJPY54410
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マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-GFPSpark タグMG52947-ANGJPY54410
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-OFPSpark タグMG52947-ANRJPY54410
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, C-Flag タグMG52947-CFJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, C-His タグMG52947-CHJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, C-Myc タグMG52947-CMJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, C-HA タグMG52947-CYJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone in cloning vectorMG52947-GJPY18140
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-Flag タグMG52947-NFJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-His タグMG52947-NHJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-Myc タグMG52947-NMJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmid, N-HA タグMG52947-NYJPY47150
マウス glutaredoxin-1 / GRX1 / GLRX Gene ORF cDNA clone expression plasmidMG52947-UTJPY47150
 発現ベクターの詳細情報
Product nameProduct name
背景

Glutaredoxin-1, also known as GRX1 and GLRX, belongs to the glutaredoxin family. Glutaredoxins are small redox enzymes that use glutathione as a cofactor. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. Glutaredoxin-1 functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Glutaredoxin-1 exists in either a reduced or an oxidized form. Glutaredoxins function as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by the enzymeribonucleotide reductase.

参考文献
  • Holmgren A. et al., 1988, FEMS Microbiol Rev. 4 (4): 271-97.
  • Holmgren A. 1988, Biochem Soc Trans. 16 (2): 95-6.
  • Holmgren A. 1989, J Biol Chem. 264 (24): 13963-6.
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