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Glutaredoxin 1 Recombinant Protein | GLRX1 recombinant protein

Recombinant Human Glutaredoxin 1

Gene Names
GLRX; GRX; GRX1
Purity
Greater than 95% as determined by SDS-PAGE.
Synonyms
Glutaredoxin 1; Recombinant Human Glutaredoxin 1; GLRX1 Human; Glutaredoxin 1 Human Recombinant; Thioltransferase; GRX; GLRX1; GRX1; GRX-1; GLRX-1; Glutathione-dependent oxidoreductase 1; Glutaredoxin-1; Thioltransferase-1; TTase-1; GLRX; MGC117407; GLRX1 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
Greater than 95% as determined by SDS-PAGE.
Form/Format
Glutaredoxin solution contains 20 mM Tris-HCl pH-8, 1mM DTT & 10% Glycerol.
Sterile Filtered clear colorless solution.
Sequence
MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ
Sequence Length
106
Preparation and Storage
Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Related Product Information for GLRX1 recombinant protein
Description: Glutaredoxin Human Recombinant produced in E Coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa.

Introduction: GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.
Product Categories/Family for GLRX1 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
11,776 Da
NCBI Official Full Name
glutaredoxin-1
NCBI Official Synonym Full Names
glutaredoxin (thioltransferase)
NCBI Official Symbol
GLRX
NCBI Official Synonym Symbols
GRX; GRX1
NCBI Protein Information
glutaredoxin-1; TTase-1; thioltransferase-1
UniProt Protein Name
Glutaredoxin-1
UniProt Gene Name
GLRX
UniProt Synonym Gene Names
GRX; TTase-1
UniProt Entry Name
GLRX1_HUMAN

NCBI Description

This gene encodes a member of the glutaredoxin family. The encoded protein is a cytoplasmic enzyme catalyzing the reversible reduction of glutathione-protein mixed disulfides. This enzyme highly contributes to the antioxidant defense system. It is crucial for several signalling pathways by controlling the S-glutathionylation status of signalling mediators. It is involved in beta-amyloid toxicity and Alzheimer's disease. Multiple alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Aug 2011]

Uniprot Description

GLRX1: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Belongs to the glutaredoxin family.

Protein type: Oxidoreductase

Chromosomal Location of Human Ortholog: 5q14

Cellular Component: mitochondrion; cytosol; nucleus

Molecular Function: electron carrier activity; protein N-terminus binding; glutathione disulfide oxidoreductase activity

Biological Process: nucleobase, nucleoside and nucleotide metabolic process; nucleobase, nucleoside and nucleotide interconversion; cell redox homeostasis; positive regulation of membrane potential

Research Articles on GLRX1

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Product Notes

The GLRX1 glrx (Catalog #AAA143601) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ. It is sometimes possible for the material contained within the vial of "Glutaredoxin 1, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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