Recombinant Mouse Three-Prime Repair Exonuclease 1 (TREX1) Protein (His&Myc)

Name: Recombinant Mouse Three-Prime Repair Exonuclease 1 (TREX1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04950P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Three-Prime Repair Exonuclease 1 (TREX1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q91XB0
Target Symbol	TREX1
Synonyms	Trex1; Three-prime repair exonuclease 1; EC 3.1.11.2; 3'-5' exonuclease TREX1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MGSQTLPHGHMQTLIFLDLEATGLPSSRPEVTELCLLAVHRRALENTSISQGHPPPVPRPPRVVDKLSLCIAPGKACSPGASEITGLSKAELEVQGRQRFDDNLAILLRAFLQRQPQPCCLVAHNGDRYDFPLLQTELARLSTPSPLDGTFCVDSIAALKALEQASSPSGNGSRKSYSLGSIYTRLYWQAPTDSHTAEGDVLTLLSICQWKPQALLQWVDEHARPFSTVKPMYGTPATTGTTNLRPHAATATTPLATANGSPSNGRSRRPKSPPPEKVPEAPSQEGLLAPLSLLTLLTLAIATLYGLFLASPGQ
Expression Range	1-314aa
Protein Length	Full length
Mol. Weight	41.1 kDa
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.
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	Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair.
Subcellular Location	Nucleus. Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Retained in the cytoplasm through the C-terminal region. In response to DNA damage, translocates to the nucleus where it is specifically recruited to replication foci. Translocation to the nucleus also occurs during GZMA-mediated cell death.
Protein Families	Exonuclease superfamily, TREX family
Database References	KEGG: mmu:22040 STRING: 10090.ENSMUSP00000050971 UniGene: PMID: 28598415 the cell-cycle-dependent post-translation modification of TREX1 regulates its interaction with OST. PMID: 28297665 The effect of topical TREX1 knockdown and local interferon production on HIV transmission in human cervicovaginal explants and humanized mice, is reported. PMID: 27184854 data do not support the concept of retroelement-derived cDNA as key triggers of systemic autoimmunity in Trex1-deficient humans and mice PMID: 28835460 Trex1 expression in dendritic cells is essential to prevent breakdown of self-tolerance ensuing from aberrant detection of endogenous DNA. PMID: 27511730 Data show that oligosaccharyltransferase (OST) activity is dysregulated in three prime exonuclease 1 knockout (Trex1-/-) cells. PMID: 26320659 Data show that cyclic GMP-AMP synthase (cGAS) is essential for all aspects of the autoimmune disease in 3' repair exonuclease Trex1 knockout mice. PMID: 26223655 Dysfunctional dsDNA degradation by TREX1 D18N induces disease in mice that recapitulates many characteristics of human lupus. PMID: 25848017 knocking out the DNA sensor cyclic GMP-AMP synthase completely abrogates spontaneous induction of IFN-stimulated genes in TREX1-deficient cells. PMID: 24813208 Spontaneous type I INF dependent cutaneous pathology in TREX1 deficiency illustrates common pathogenetic pathway in chilblain lupus. PMID: 24270665 Upon proinflammatory stimulation, Trex1(-/-) macrophages increase CD86, TNF-alpha & IFN-alpha production, & Ag presentation to CD4(+) T cells, but decrease apoptotic T cell clearance. Trex1 is a negative regulator of macrophage inflammatory activation. PMID: 24218451 Oxidized DNA Is less susceptible to TREX1 degradation; the oxidized base 8-hydroxyguanosine, a marker of oxidative damage in DNA, potentiated cytosolic immune recognition by decreasing its susceptibility to 3' repair exonuclease 1 -mediated degradation PMID: 23993650 regulates lysosomal biogenesis and interferon-independent activation of antiviral genes PMID: 23160154 The structures of the mutant TREX1 proteins provide insight into the dysfunction relating to human disease. PMID: 22071149 TREX1 bound to cytosolic HIV DNA and digested excess HIV DNA that would otherwise activate interferon expression via a pathway dependent on the kinase TBK1, the adaptor STING and the transcription factor IRF3 PMID: 20871604 Trex1(-/-) mice exhibit a dramatically reduced survival and develop inflammatory myocarditis leading to progressive, often dilated, cardiomyopathy and circulatory failure PMID: 15254239 Study defines Trex1 as an essential negative regulator of the IFN-stimulatory DNA response and delineate the genetic pathway linking Trex1 deficiency to lethal autoimmunity. PMID: 18724932 Study showed that GFP-TREX1-(1-307) lacking the C-terminal seven amino acids localizes in a perinuclear pattern. PMID: 19442247

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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.