Recombinant Human Transcription Intermediary Factor 1-Beta (TRIM28) Protein (GST)

Name: Recombinant Human Transcription Intermediary Factor 1-Beta (TRIM28) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08426P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Transcription Intermediary Factor 1-Beta (TRIM28) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13263
Target Symbol	TRIM28
Synonyms	E3 SUMO protein ligase TRIM28; E3 SUMO-protein ligase TRIM28; FLJ29029; KAP 1; KAP-1; KRAB associated protein 1; KRAB interacting protein 1; KRAB-associated protein 1; KRAB-interacting protein 1; KRIP 1; KRIP-1; KRIP1; Nuclear corepressor KAP 1; Nuclear corepressor KAP-1; RING finger protein 96; RNF96; TF1B; TIF1 beta; TIF1-beta; TIF1B; TIF1B_HUMAN; Transcription intermediary factor 1 beta; Transcription intermediary factor 1-beta; Trim28; Tripartite motif containing 28; tripartite motif containing protein 28; Tripartite motif-containing protein 28
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	PGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRV
Expression Range	22-291aa
Protein Length	Partial
Mol. Weight	55.8kDa
Research Area	Transcription
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	Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway. Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions. Acts as a corepressor for ZFP568.; (Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1.
Subcellular Location	Nucleus.
Protein Families	TRIM/RBCC family
Database References	HGNC: 16384 OMIM: 601742 KEGG: hsa:10155 STRING: 9606.ENSP00000253024 UniGene: PMID: 29290627 Data suggest that retention of SMARCAD1 in nucleus is dependent on interaction of CUE1 domain of SMARCAD1 with RBCC domain of KAP1; these studies were conducted with recombinant proteins expressed in mouse embryonic stem cell line and human somatic cell line. (SMARCAD1 = ATP-dependent helicase-1; KAP1 = KRAB-interacting protein-1) PMID: 29284678 Comparison of chromatin immunoprecipitation and high throughput nucleotide sequencing data and a reference motif set for human KRAB C2H2 zinc finger proteins has been reported. PMID: 29146583 Genes co-repressed by TRIM28 and FAM208A are evolutionarily young, or exhibit tissue-specific expression, are enriched in young L1s, and display evidence for regulation through LTR promoters. Finally, we demonstrate that the HUSH complex is also required to repress L1 elements in human cells. PMID: 29728366 Authors identify a viral mechanism for the counteraction of KAP1 in which interference with the KAP1 phosphatase protein phosphatase 1 (PP1) by the AAV2 Rep proteins mediates enhanced phosphorylation of KAP1-S824 and thus relief from KAP1 repression. PMID: 29581310 Evaluation of the potential mechanism demonstrated that TRIM28 promoted cervical cancer cell growth by activating the mammalian target of rapamycin (mTOR) signaling pathway. In support of this finding, TRIM28-induced cell proliferation was abolished by treatment with everolimus, a specific mTOR inhibitor PMID: 29393469 TRIM28 employs KRAB-ZNFs to evoke epigenetic silencing of its target differentiation genes via H3K9me3 and DNA methylation. PMID: 29198826 Study describes germline mutations and loss of function of TRIM28 in familial Wilms tumours, along with somatic loss of function in a non-familial Wilms tumour. Inactivation of TRIM28 provides the molecular basis for defining a previously described subtype of Wilms tumour, that has early age of onset and excellent prognosis. PMID: 29912901 Study identified TRIM28 among REST-interacting proteins, and suggested functional links between REST and TRIM28 during neuronal development and differentiation via induction of CTNND2 expression. PMID: 27976729 Data indicate a mechanism in breast cancer cells that tripartite motif-containing 28 protein (TRIM28) enhances metastasis by stabilizing TWIST1, suggesting that targeting TRIM28 could be an efficacious strategy in breast cancer treatment. PMID: 27412325 Gamma-H2AX, phosphorylated KAP-1 and 53BP1 play an important role in the repair of heterochromatic radon-induced DNA double-strand breaks. PMID: 27922110 Our data demonstrate that the downregulation of TRIM28 gene expression reduced the ability of CSCs to self-renew that resulted in significant reduction of tumor growth. Loss of function of TRIM28 leads to dysregulation of cell cycle, cellular response to stress, cancer cell metabolism, and inhibition of oxidative phosphorylation. PMID: 27845900 Cell proliferation and apoptosis were almost completely abolished in the PAa cells cotreated with TRIM28 siRNA and etoposide following knockdown of E2F1. The results of our study demonstrated that the combination of TRIM28 siRNA and etoposide may be effective against nonsmall cell lung cancer (NSCLC)and has the potential of being a new therapeutic tool for future treatment. PMID: 28498400 The authors found that TRIM28 regulates alpha-Synuclein and tau nuclear levels and that its reduction rescues toxicity in animal models of tau- and alpha-Synuclein-mediated degeneration. PMID: 27779468 TRIM28 represses Endogenous retroviruses and consequently regulates the expression of neighboring genes. PMID: 28052240 it is primarily peroxide-induced p38 MAPK that mediates Ser473 phosphorylation and activation of TIF1beta to enable more efficient DNA repair to assist in tumor cell survival against exogenous ROS PMID: 28864417 TRIM28 acts as a central factor in controlling endothelial inflammatory responses and angiogenic activities by retaining expression of TNFR-1 and -2 and VEGF receptor 2 in endothelial cells PMID: 28159803 TRIM28 depletion repressed EZH2 recruitment to chromatin and expression of this gene set, in parallel with decreased CD44(hi)/CD24(lo) mammosphere formation. PMID: 28068325 These findings provide a unique context in which ataxia telangiectasia mutated proteins modify KAP1 to regulate persistence of a herpesvirus in humans PMID: 28249048 OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1beta, and a purified OGA-SPT5-TIF1beta complex has elongation properties. PMID: 27601472 that KAP1 phosphorylation is decreased following recruitment of PP2A by URI. PMID: 27780869 Taken together, these results suggest that PARIS and PIASy modulate PGC-1a gene transcription through distinct molecular mechanisms. PMID: 27086851 a role for TRIM28 on EMT, drug resistance, and stemness in addition to the already reported protumorigenic actions in breast and other cancers. PMID: 28381187 Data suggest that TRIM28 regulates the expression of a subset of lncRNAs. PMID: 27432546 we revealed that KAP1 was overexpressed in HCC patients and also an independently biomarker for the overall survival rate prediction of patients with HCC. It appeared that KAP1 was involved into the tumor progression process. PMID: 27095111 Combined effect of dynamic recruitment of RNF4 to KAP1 regulates the relative occupancy of 53BP1 and BRCA1 at double-strand break sites to direct DNA repair in a cell cycle-dependent manner. PMID: 26766492 These results indicate that over-expression of TRIM28 is associated with poor outcome in glioma patients. PMID: 26476730 Adipose tissue transcriptome analyses in children indicate that humans, like mice cluster into distinct sub-populations, stratifying according to Trim28 expression, transcriptome organization, and obesity-associated imprinted gene dysregulation. PMID: 26824653 KAP1 controls 7SK snRNP delivery to promoter-proximal regions to facilitate "on-site" P-TEFb activation and Pol II elongation. PMID: 26725010 KAP1 binds to the viral E1B-55K protein, promoting its SUMO modification, therefore illustrating a crucial step for efficient viral replication. PMID: 26537675 Data show that tripartite motif-containing 28 protein (TRIM28) and beta-actin were up-regulated in the glioblastoma multiforme (GBM) stem-like cells compared to the controls. PMID: 25419715 study suggests a SIRT1-KAP1 regulatory mechanism for HR-NHEJ repair pathway choice PMID: 25905708 Study indicates that TRIM28 appears to play a unique and essential role in transcriptional elongation and DNA repair by pausing and stabilizing Pol II. [Review] PMID: 26293668 SET interacts with the Kruppel-associated box (KRAB)-associated co-repressor KAP1, and its overexpression results in the sustained retention of KAP1 and Heterochromatin protein 1 (HP1) on chromatin PMID: 25818296 Human cytomegalovirus latency in human CD34(+) hematopoietic stem cells reflects the recruitment on the viral genome of KAP1, a master co-repressor, together with HP1 and the SETDB1 histone methyltransferase, which results in transcriptional silencing. PMID: 25846574 Nrf2 interaction with KSHV LANA-1 and the host KAP1 repress viral lytic gene expression. PMID: 25995248 results suggest a model in which Trim28 is a tumor suppressor early in the transformation process in lung cancer, but in later stages it functions as an oncogene PMID: 24983967 Inhibition of LMP1-induced protein sumoylation abrogates the binding of KAP1 to Epstein-Barr Virus promoters. PMID: 25948750 TRIM28 is an E3 ligase for ARF-mediated SUMOylation of NPM1. PMID: 26055329 KAP1 expression correlated significantly with clinical stage, pathological grade and metastases in ovarian cancer. PMID: 25548895 Identify a nuclear localization signal within the 462-494 amino acid region of TRIM28 that overlaps with its HP1 binding site. GST-pulldown experiments revealed the interaction of the arginine-rich TRIM28 NLS with various importin alpha subtypes. PMID: 25960296 Data show that RRP1B regulates metastasis associated gene expression by interacting with the transcriptional corepressors TRIM28 and HP1a, which act by recruiting chromatin-modifying enzymes. PMID: 25092915 successfully established stable pcDNA5/FRT/TO-KAP1-HEK293 cell line, which can express KAP1 inducibly. This inducible cell line might be very useful for KAP1 functional studies. PMID: 26081272 TRIM28 regulates senescence and affects the induction of the senescence-associated secretory phenotype. PMID: 25160591 KAP-1 is overexpressed and correlates with increased metastatic ability in pancreatic cancer.KAP-1 may promote metastasis in pancreatic cancer by regulating the epithelial-mesenchymal transition. PMID: 24861921 Results show that KAP1-mediated stimulation of multiple KRAB-ZNF contributes to the growth and metastasis of breast cancer. PMID: 25421577 TRIM28-mediated regulation is responsible for controlling a very broad range of human-specific endogenous retroelements. PMID: 24879559 MAGE proteins bind to KAP1, a gene repressor and ubiquitin E3 ligase which also binds KRAB domain containing zinc finger transcription factors (KZNFs), and MAGE expression may affect KZNF mediated gene regulation. PMID: 25107531 the ARM dynamically regulates the SIM-dependent recruitment of targets to RNF4, which could be critical to dynamically fine-tune the abundance of Ser(P)-824-SUMO-KAP1 and, potentially, other SUMOylated proteins during DNA damage response. PMID: 24907272 TRIM28 is a new factor that modulates Pol II pausing and transcriptional elongation at a large number of mammalian genes. PMID: 25173174

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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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