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

Name: Recombinant Human Three-Prime Repair Exonuclease 1 (TREX1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07974P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Three-Prime Repair Exonuclease 1 (TREX1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9NSU2
Target Symbol	TREX1
Synonyms	TREX1; Three-prime repair exonuclease 1; EC 3.1.11.2; 3'-5' exonuclease TREX1; Deoxyribonuclease III; DNase III
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MGPGARRQGRIVQGRPEMCFCPPPTPLPPLRILTLGTHTPTPCSSPGSAAGTYPTMGSQALPPGPMQTLIFFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEITGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALERASSPSEHGPRKSYSLGSIYTRLY
Expression Range	1-242aa
Protein Length	Partial
Mol. Weight	32.7 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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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.
Protein Families	Exonuclease superfamily, TREX family
Database References	HGNC: 12269 OMIM: 152700 KEGG: hsa:11277 STRING: 9606.ENSP00000390478 UniGene: Hs.707026
Associated Diseases	Aicardi-Goutieres syndrome 1 (AGS1); Systemic lupus erythematosus (SLE); Chilblain lupus 1 (CHBL1); Vasculopathy, retinal, with cerebral leukodystrophy (RVCL)
Tissue Specificity	Detected in thymus, spleen, liver, brain, heart, small intestine and colon.

Gene Functions References

data identifies miR-103 regulation of TREX1 as a potent modulator of the tumour microenvironment. PMID: 27886180
Thus, the intracellular level of TREX1 pivotally modulates innate immune induction by HIV-1. Partial HIV-1 genomes are the TREX1 target and are sensed by cGAS. PMID: 29769349
TREX1-deficient neurons also exhibited increased apoptosis and formed three-dimensional cortical organoids of reduced size. PMID: 28803918
Homozygote R114C mutation in TREX1 gene was shown in two siblings, one with chilblains and another with chilblains accompanied with cerebral vasculitis. PMID: 28919362
TREX1 frame-shift mutations induce autoantibodies against mostly non-nuclear antigens, patients carrying these mutations are likely be ANA negative PMID: 28325644
The activation of interferon-induced genes is controlled by the JAK-STAT system; therefore, JAK inhibitors were successfully used in several cases to treat type 1 interferonopathies. Experience with this treatment modality is continuously growing. PMID: 28389709
TheTREX1 and STING, which are opposing regulators of the cytosolic DNA-sensing pathway. PMID: 28475463
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
Aicardi-Goutieres syndrome protein TREX1 suppresses L1 and maintains genome integrity through exonuclease-independent ORF1p depletion. PMID: 28334850
Analysis of mRNA expression profiles in breast tumors demonstrates that those with lower Trex1 and higher BLM and EXO1 expression levels are associated with poor prognosis PMID: 28279982
showed that patients with SSc or SLE have AAb against EphB2, a protein involved in angiogenesis, and THEX1, a 3'-5' exoribonuclease involved in histone mRNA degradation. PMID: 27617966
The expression of TREX1 was closely related to the cytobiology characteristics of osteosarcoma stem cell. PMID: 27881153
Heterozygous mutations in TREX1 were reported in SLE patients. PMID: 26150267
synonymous variant p.(Tyr177) associated with an increased risk of systemic scleroderma; association strongest in patients with limited cutaneous scleroderma, in particular in those with more severe digital vascular disease PMID: 27574969
This study reviewed that Neurologic Phenotypes Associated with Mutations in TREX1 in patients with Aicardi-Goutieres Syndrome. PMID: 27643693
Aicardie-Goutieres syndrome is described in a patient with a homozygous p.Arg114His mutation in the TREX1 gene. PMID: 28089741
CDK11 was found associated with the TREX/THOC, which recruited this kinase to DNA. Once at the viral genome, CDK11 phosphorylated serines at position 2 in the CTD of RNAPII, which increased levels of cleavage and polyadenylation factors at the HIV 3' end. In its absence, cleavage of viral transcripts was greatly attenuated. PMID: 26567509
Aicardi-Goutieres syndrome 1 is caused by mutations in the three prime repair exonuclease 1 gene (TREX1, MIM 606609). PMID: 25906927
Functional analysis of retinal vasculopathy with cerebral leukodystrophy-associated TREX1 T270 frameshift-mutated fibroblasts showed a prevalent localization of the protein in the cytosol, rather than in the perinuclear region PMID: 25213617
Here we briefly describe the human diseases so-far associated with mutations in TREX1, which include Aicardi-Goutieres syndrome, familial chilblain lupus, systemic lupus erythematosus and retinal vasculopathy with cerebral leukodystrophy PMID: 25731743
Studies indicate that the biosensing strategy is based on the protection of DNA duplex from exonuclease III (Exo III)-mediated digestion by specific binding of estrogen receptor (ER) to its DNA response element. PMID: 23681011
The authors observed that the minor allele of SNP rs3135941 in Trex1 is associated with faster HIV-1 disease progression. PMID: 25162766
Unlike previously reported TREX1 mutations, which affect Exo I or Exo II domains, the mutation presented here alters the Exo III domain, suggesting a role of mutations within the catalytic Exo domains in the pathogenesis of familial chilblain lupus PMID: 25517357
Data suggest that the 3'-5' DNA exonuclease TREX1 may contribute to stabilization of poly(ADP-ribose) polymerase-1 (PARP1) levels in the DNA damage response and its activity. PMID: 25278026
knocking out the DNA sensor cyclic GMP-AMP synthase completely abrogates spontaneous induction of IFN-stimulated genes in TREX1-deficient cells. PMID: 24813208
Data indicate that the single nucleotide polymorphism rs3135945 was significantly associated with HIV infection, emphasizing the involvement of TREX-1 in the anti-HIV response. PMID: 23773365
This study contributes to the demonstration that TREX1 is involved in autoimmune diseases and proposes that the spectrum of involved autoimmune diseases can be broader and includes systemic sclerosis . PMID: 24224166
Spontaneous type I INF dependent cutaneous pathology in TREX1 deficiency illustrates common pathogenetic pathway in chilblain lupus. PMID: 24270665
These data provide compelling evidence for the required TREX1 dimeric structure for full catalytic function. PMID: 24616097
A nationwide survey of Aicardi-Goutieres syndrome patients identifies a strong association between dominant TREX1 mutations and chilblain lesions in Japan. PMID: 24300241
Screening of our patient cohort yielded heterozygous TREX1 mutations in two patients with early-onset cerebrovascular disease PMID: 23881107
TREX1 mutation is not a common cause of hereditary small vessel diseases of the brain PMID: 23602593
TREX1 post-translational modification indicates an additional mechanism by which mutations disrupt TREX1 biology, leading to human autoimmune disease. PMID: 23979357
TREX1 gene variants confer an increased risk for the development of systemic lupus erythematosus. PMID: 24034389
TREX1 knockdown resulted in enhanced cell death following nimustine. PMID: 23578789
Aicardi-Goutieres syndrome and familial chilblain lupus can be caused by a heterozygous TREX1 p.Asp18Asn mutation. PMID: 22829693
Despite its central role in the HIV-1 infection process, genetic diversity at TREX1 is not a major determinant of susceptibility to infection in humans. PMID: 22526516
The structures of the mutant TREX1 proteins provide insight into the dysfunction relating to human disease. PMID: 22071149
TREX1 residues in one protomer contributing to DNA degradation catalyzed in the opposing protomer and help to explain the dimeric TREX1 structure required for full catalytic competency. PMID: 21937424
failure to degrade genomic dsDNA is a principal pathway of immune activation in TREX1-mediated autoimmune disease. PMID: 21808053
data confirm and expand previous reports and provide additional support for the involvement of TREX1 in lupus pathogenesis PMID: 21270825
A single case of a heterozygous TREX1 mutation has been associated with Aicardi-Goutieres syndrome, an encephalopathy often resembling congenital infection. PMID: 20799324
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
The deficiency of Trex-1 in rheumatoid arthritis synovial fibroblasts allows a longer half-life of gene products encoded by active endogenous L1 retrotransposons. PMID: 20496420
TREX1 mutations do not play a role in the pathogenesis of Sporadic inclusion body myositis. PMID: 20192983
TREX1 may act in degrading DNA in all cell types undergoing a dying process before phagocytosis occurs. PMID: 19617005
TREX1, encoding the major mammalian 3' --> 5' DNA exonuclease, is the AGS1 gene, and AGS-causing mutations result in abrogation of TREX1 enzyme activity. PMID: 16845398
Heterozygous mutations in TREX1 cause familial chilblain lupus and dominant Aicardi-Goutieres syndrome. PMID: 17357087

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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.

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