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>   home   >   Products   >   Peptides   >   Blocking Peptides   >   TXNL1 (TRP32/TrxL) Antibody (N-term) Blocking peptide   

TXNL1 (TRP32/TrxL) Antibody (N-term) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession O43396
Clone Names 3121805
Peptide ID 3121805
Additional Information
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.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
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; 64 IntAct; O43396; 12 MINT; O43396; - STRING; 9606.ENSP00000217515; - iPTMnet; O43396; - PhosphoSitePlus; O43396; - BioMuta; TXNL1; - OGP; O43396; - REPRODUCTION-2DPAGE; IPI00305692; - EPD; 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; ENSGT00530000063008; - HOGENOM; HOG000189802; - HOVERGEN; HBG055982; - InParanoid; O43396; - OMA; PIFEMFP; - OrthoDB; EOG091G0G71; - PhylomeDB; O43396; - TreeFam; TF314399; - ChiTaRS; TXNL1; human EvolutionaryTrace; O43396; - GeneWiki; TXNL1; - GenomeRNAi; 9352; - PRO; PR:O43396; - Proteomes; UP000005640; Chromosome 18 Bgee; ENSG00000091164; - CleanEx; HS_TXNL1; - 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:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central GO; GO:0047134; F:protein-disulfide reductase activity; IBA:GO_Central GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central 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
Research Areas
Citations (0)

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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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$ 80.00
Cat# BP1336a
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