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TXNL1 (TRP32/TrxL) Antibody (N-term) Blocking peptide
Synthetic peptide
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| Primary Accession | O43396 |
|---|---|
| Clone Names | 3121805 |
| Peptide ID | 3121805 |
| Other Names | Thioredoxin-like protein 1, 32 kDa thioredoxin-related protein, TXNL1, TRP32, TXL, TXNL |
|---|---|
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1336a was selected from the N-term region of human TrxL. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | TXNL1 |
|---|---|
| Synonyms | TRP32, TXL, TXNL |
| Function | Active thioredoxin with a redox potential of about -250 mV. |
| Cellular Location | Cytoplasm. Nucleus. Note=At least 85% of the cellular TXNL1 is proteasome-associated |
| Tissue Location | Ubiquitous. EMBL; AF003938; AAC39599.1; -; mRNA EMBL; AF052659; AAC39898.1; -; mRNA EMBL; AF143897; AAF66676.1; -; Genomic_DNA EMBL; AF143890; AAF66676.1; JOINED; Genomic_DNA EMBL; AF143891; AAF66676.1; JOINED; Genomic_DNA EMBL; AF143892; AAF66676.1; JOINED; Genomic_DNA EMBL; AF143893; AAF66676.1; JOINED; Genomic_DNA EMBL; AF143894; AAF66676.1; JOINED; Genomic_DNA EMBL; AF143895; AAF66676.1; JOINED; Genomic_DNA EMBL; AF143896; AAF66676.1; JOINED; Genomic_DNA EMBL; AF051896; AAC05830.1; -; mRNA EMBL; BC001156; AAH01156.1; -; mRNA CCDS; CCDS11961.1; - PIR; JC5938; JC5938 RefSeq; NP_004777.1; NM_004786.2 RefSeq; XP_016881582.1; XM_017026093.1 UniGene; Hs.114412; - PDB; 1GH2; X-ray; 2.22 A; A=2-108 PDB; 1WWY; NMR; -; A=122-279 PDBsum; 1GH2; - PDBsum; 1WWY; - ProteinModelPortal; O43396; - SMR; O43396; - BioGrid; 114755; 70 IntAct; O43396; 11 MINT; O43396; - STRING; 9606.ENSP00000217515; - iPTMnet; O43396; - PhosphoSitePlus; O43396; - BioMuta; TXNL1; - OGP; O43396; - REPRODUCTION-2DPAGE; IPI00305692; - EPD; O43396; - jPOST; O43396; - PaxDb; O43396; - PeptideAtlas; O43396; - PRIDE; O43396; - ProteomicsDB; 48922; - TopDownProteomics; O43396; - DNASU; 9352; - Ensembl; ENST00000217515; ENSP00000217515; ENSG00000091164 Ensembl; ENST00000590954; ENSP00000464918; ENSG00000091164 GeneID; 9352; - KEGG; hsa:9352; - CTD; 9352; - DisGeNET; 9352; - EuPathDB; HostDB:ENSG00000091164.12; - GeneCards; TXNL1; - HGNC; HGNC:12436; TXNL1 HPA; CAB016446; - HPA; HPA002828; - HPA; HPA002829; - MIM; 603049; gene neXtProt; NX_O43396; - OpenTargets; ENSG00000091164; - PharmGKB; PA134967488; - eggNOG; KOG0908; Eukaryota eggNOG; ENOG410YQ2G; LUCA GeneTree; ENSGT00940000156170; - HOGENOM; HOG000189802; - HOVERGEN; HBG055982; - InParanoid; O43396; - OMA; PIFEMFP; - OrthoDB; 1482186at2759; - PhylomeDB; O43396; - TreeFam; TF314399; - ChiTaRS; TXNL1; human EvolutionaryTrace; O43396; - GeneWiki; TXNL1; - GenomeRNAi; 9352; - PRO; PR:O43396; - Proteomes; UP000005640; Chromosome 18 Bgee; ENSG00000091164; Expressed in 239 organ(s), highest expression level in thyroid gland ExpressionAtlas; O43396; baseline and differential Genevisible; O43396; HS GO; GO:0005737; C:cytoplasm; IDA:UniProtKB GO; GO:0005829; C:cytosol; IDA:HPA GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro Gene3D; 2.60.120.470; -; 1 InterPro; IPR008979; Galactose-bd-like_sf InterPro; IPR010400; PITH_dom InterPro; IPR037047; PITH_dom_sf InterPro; IPR036249; Thioredoxin-like_sf InterPro; IPR017937; Thioredoxin_CS InterPro; IPR013766; Thioredoxin_domain Pfam; PF06201; PITH; 1 Pfam; PF00085; Thioredoxin; 1 SUPFAM; SSF49785; SSF49785; 1 SUPFAM; SSF52833; SSF52833; 1 PROSITE; PS51532; PITH; 1 PROSITE; PS00194; THIOREDOXIN_1; 1 1: Evidence at protein level; 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Electron transport; Nucleus; Phosphoprotein; Proteasome; Redox-active center; Reference proteome; Transport INIT_MET 1 1 Removed. CHAIN 2 289 Thioredoxin-like protein 1 /FTId=PRO_0000120016 DOMAIN 2 109 Thioredoxin DOMAIN 115 285 PITH. {ECO:0000255|PROSITE- ProRule:PRU00864} MOD_RES 113 113 Phosphoserine DISULFID 34 37 Redox-active STRAND 4 7 {ECO:0000244|PDB:1GH2} HELIX 10 12 {ECO:0000244|PDB:1GH2} HELIX 13 19 {ECO:0000244|PDB:1GH2} TURN 20 22 {ECO:0000244|PDB:1GH2} STRAND 25 30 {ECO:0000244|PDB:1GH2} HELIX 35 50 {ECO:0000244|PDB:1GH2} STRAND 54 60 {ECO:0000244|PDB:1GH2} TURN 61 63 {ECO:0000244|PDB:1GH2} HELIX 65 70 {ECO:0000244|PDB:1GH2} STRAND 75 83 {ECO:0000244|PDB:1GH2} STRAND 86 94 {ECO:0000244|PDB:1GH2} HELIX 96 107 {ECO:0000244|PDB:1GH2} HELIX 127 129 {ECO:0000244|PDB:1WWY} TURN 132 134 {ECO:0000244|PDB:1WWY} STRAND 136 139 {ECO:0000244|PDB:1WWY} STRAND 142 144 {ECO:0000244|PDB:1WWY} STRAND 150 154 {ECO:0000244|PDB:1WWY} STRAND 166 182 {ECO:0000244|PDB:1WWY} STRAND 186 188 {ECO:0000244|PDB:1WWY} STRAND 193 199 {ECO:0000244|PDB:1WWY} HELIX 208 211 {ECO:0000244|PDB:1WWY} TURN 222 224 {ECO:0000244|PDB:1WWY} TURN 235 237 {ECO:0000244|PDB:1WWY} STRAND 241 248 {ECO:0000244|PDB:1WWY} STRAND 263 271 {ECO:0000244|PDB:1WWY} SEQUENCE 289 AA; 32251 MW; B2CC0BD8042225C2 CRC64; MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDTTFLESD CDEQLLITVA FNQPVKLYSM KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN VNSVTIFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH |
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Application Protocols
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Background
Thioredoxins are a group of small redox active proteins possessing a conserved active site sequence. TrxL (Thioredoxin like protein 1) has 2 distinct domains: an N terminal domain, which is 43% identical to human TXN, and a C terminal domain, which shows no homology to other proteins in the sequence databases. The active site sequence, located within the N terminal domain, is that of a thioredoxin like protein; compared to the active site sequence of TXN, it has a single amino acid substitution. Unlike other thioredoxin like proteins, TrxL does not serve as a substrate for thioredoxin reductase in an insulin assay.
References
Miranda-Vizuete, A., et al., DNA Seq. 10(6):419-424 (2000).Lee, K.K., et al., J. Biol. Chem. 273(30):19160-19166 (1998).Miranda-Vizuete, A., et al., Biochem. Biophys. Res. Commun. 243(1):284-288 (1998).
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Cat# BP1336a
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