Recombinant Human Transcription Factor A, Mitochondrial (TFAM) Protein (His)

Name: Recombinant Human Transcription Factor A, Mitochondrial (TFAM) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06812P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Transcription Factor A, Mitochondrial (TFAM) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q00059
Target Symbol	TFAM
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SSVLASCPKKPVSSYLRFSKEQLPIFKAQNPDAKTTELIRRIAQRWRELPDSKKKIYQDAYRAEWQVYKEEISRFKEQLTPSQIMSLEKEIMDKHLKRKAMTKKKELTLLGKPKRPRSAYNVYVAERFQEAKGDSPQEKLKTVKENWKNLSDSEKELYIQHAKEDETRYHNEMKSWEEQMIEVGRKDLLRRTIKKQRKYGAEEC
Expression Range	43-246aa
Protein Length	Full Length of Mature Protein
Mol. Weight	28.5 kDa
Research Area	Cardiovascular
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	Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA.
Subcellular Location	Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid.
Database References	HGNC: 11741 OMIM: 600438 KEGG: hsa:7019 STRING: 9606.ENSP00000420588 UniGene: PMID: 28276514 CTGF can reduce glycolysis and mitochondrial OXPHOS pathways by increasing mtTFA protein degradation and in turn reduces cancer migration and invasion in oral squamous cell carcinoma (OSCC). PMID: 28438434 radiation stimulated the levels of TFAM mRNA and protein. PMID: 29856906 Two tag SNPs of TFAM and POLG were associated with multibacillary leprosy in Han Chinese from Southwest China. PMID: 28958595 Data revealed that TFAM expression level was regulated by TP73-AS1/miR-200a axis in breast cancer cells. PMID: 28639399 Study clearly shows that hTFAM efficiently breaks the mitochondria-mediated vicious cycle in both Alzheimer's disease (AD) model neurons and mouse brains, resulting in an effective improvement of the AD pathophysiology including Abeta accumulation and cognitive dysfunction. PMID: 27897204 these findings establish a new link between HIF-2alpha and MAPK-signaling that mediates the adaptive regulation of mitochondrial gene expression under low oxygen tension. PMID: 28709643 the results presented in this study obviously provided the evidence that TFAM was upregulated in glioma cell line and glioma tissue specimens. Therefore TFAM may be a novel diagnostic marker and therapeutic target for glioma and other cancer. PMID: 28440425 Biotinylated TMP interacts with TFAM. PMID: 28465355 TFAM polymorphisms (rs1937, rs1049432, and rs11006132) as well as their haplotypes did not show significant association with aggressiveness of prostate cancer in overweight or obese men. PMID: 27843028 results suggest a nucleation-cooperativity-based mechanism for sensitive detection of mitochondrial DNA and pathogen genomes, and identify HMGB/TFAM proteins as DNA-structuring host factors; they provide an explanation for the peculiar cGAS dimer structure and suggest that cGAS preferentially binds incomplete nucleoid-like structures or bent DNA PMID: 28902841 p53 might incrase mtDNA copy number through its regulation on TFAM expression via TFAMpromoter. PMID: 27732955 TFAM is a gene regulator that acts to mitigate calcium mishandling and ROS production by wrapping around mitochondrial DNA complexes. TFAM's regulatory functions over serca2a, NFAT, and Lon protease contribute to cardiomyocyte stability. [review] PMID: 27166683 The results suggest that a high mtTFA expression is a useful marker for tumor progression and a poor prognosis in left-sided colorectal cancer patients. PMID: 29277826 Study reports crystal structures of human mitochondrial transcription initiation complexes assembled on both light and heavy strand promoters. The structures reveal how transcription factors TFAM and TFB2M assist mitochondrial RNA polymerase to achieve promoter-dependent initiation. PMID: 29149603 TFAM is essential for transcription, replication and packaging of mtDNA into nucleoids. Tfam knockout mice display embryonic lethality secondary to severe mtDNA depletion. In this report, for the first time, we associate a homozygous variant in TFAM with a novel mtDNA depletion syndrome. PMID: 27448789 Tissue microarray (TMA) data showed that elevated expression of TFAM was related to the histological grade and TNM stage of NSCLC patients. PMID: 26820294 The authors did not find statistically significant differences in the genotype frequencies for the TFAM +35G/C polymorphism between women with polycystic ovary syndrome and controls and found that mtDNA copy number is not associated with TFAM+35G/C SNP in polycystic ovary syndrome patients. PMID: 29030253 Alleles in mitochondrial transcription factor A (TFAM) and AP endonuclease 1 (APE1) are associated with reduced cognitive performance. PMID: 28242328 In vivo, AICAR significantly reduced osteosarcoma growth without apparent body weight loss and AICAR increased both mitochondrial proliferation and apoptotic activity in treated tumor tissues. AICAR showed anticancer effects in osteosarcoma cells through an AMPK-dependent peroxisome proliferatoractivated receptor-gamma coactivator-1alpha (PGC-1alpha)/mitochondrial transcription factor A (TFAM)/mitochondrial pathway PMID: 27878239 the present study identified the interaction of miR-590-3p and TFAM in colon cancer. TFAM was identified as a target of miR-590-3p, and miR-590-3p enhanced the proliferation of SW480 cells. PMID: 27878255 The results of the present study provided evidence that resistance to cisplatin chemotherapy in ERpositive breast cancer may be through TFAM and indicated that TFAM may be a target for chemoresistance in patients with breast cancer. PMID: 27779689 miR-199a-3p is able to attenuate cisplatin resistance in breast cancer cells through inhibiting TFAM expression. PMID: 28126676 We conducted a meta-analysis of studies involving CHAT, TFAM, and VR22 polymorphisms and Alzheimer disease susceptibility. For TFAM and VR22, no significant association was detected in studied single-nucleotide polymorphisms (SNPs).Rs1937 and rs2306604 of TFAM, are not significantly associated with AD risk. PMID: 27272392 Results showed that TFAM formed oligomers in mitochondria by in situ chemical cross-linking and suggested the importance of the dimerization of TFAM molecules in the distribution of mtDNA in cells. PMID: 26445116 Report failed upregulation of TFAM protein and mitochondrial DNA in oxidatively deficient fibers in skeletal muscle of chronic obstructive pulmonary disease patients. PMID: 26893822 our results revealed that stimulation of mitochondrial biogenesis by carvedilol resulted in functional gain of the mitochondria by showing increased oxygen consumption and mitochondrial respiratory rate. PMID: 26797282 Data show that mtTFA proteins are highly expressed in cancer and drug-resistant cells compared to normal cells, and the mtTFA expression is upregulated by signals of oxidative and DNA damage stress in cancer cells. [review] PMID: 26307971 TFAM overexpression suppressed mitoROS and their upregulation in rat cardiomyocytes. PMID: 25822152 TFAM dimerization enhances mitochondrial DNA compaction by promoting looping of the DNA. PMID: 24435062 The combination of strong mtTFA expression and a high survivin index may predict a poor prognosis in patients with pancreatic ductal adenocarcinoma PMID: 25108120 expression of PGC1alpha and TFAM varies between ovarian carcinoma subtypes; clear-cell carcinoma consists of undetectability of PGC1alpha/TFAM, and low ERalpha/Ki-67. high-grade serous carcinomas had a converse state of PGC1alpha/TFAM, ERalpha positivity and high Ki-67 index PMID: 25243473 Methylation of TFAM promoters changed 2 days after gastric bypass. PMID: 24837562 These data disclose a novel mechanism by which ERK1/2 regulates mitochondrial function through direct phosphorylation of TFAM. PMID: 24768991 indicating that miRNA-214 and MTFA may become important candidates for developing promising therapeutic strategies for the treatment of cervical cancer PMID: 25556274 Data suggest that miitochondrial transcription factor A (mtTFA) may be a novel target for the treatment of pancreatic ductal adenocarcinoma (PDAC). PMID: 24622070 The results suggest that the expression of mtTFA mRNA and protein is down-regulated in the lung tissue from the COPD patients with squamous cell lung cancer, and the level of mtTFA protein is related to apoptosis of pulmonary vascular endothelial cells. PMID: 24367550 The mitochondria targeting sequence-deficient hTFAM also repressed Tfam promoter activity to the same degree as hTFAM. PMID: 24875355 These data show that the TFAM SNP rs2306604 A allele may be a risk factor for Parkinson's disease dementia, particularly in males, but not for dementia with Lewy bodies PMID: 24184878 The results reveal the organization of TFAM, POLRMT and TFB2M around the light-strand promoter and represent the first structural characterization of the entire mitochondrial transcriptional initiation complex. PMID: 24413562 results demonstrate that TFAM uniformly coats the whole mitochondrial genome, with no evidence of robust TFAM binding to the nuclear genome PMID: 23991223 Taken together, our data suggested that TFAM plays a crucial role in regulating mtDNA amplification and mitochondrial biogenesis under IR conditions. PMID: 23645454 overexpression of miRNA-23b in U251 cells markedly inhibited the proliferation, cell cycle progression, migration and colony formation, while overexpression of TFAM significantly enhanced these biological processes PMID: 24002170 In cells with normal mitochondrial DNA levels, phosphorylated TFAM is degraded by Lon. PMID: 23201127 TFAM protein sliding and DNA denaturation are essential for mitochondrial DNA organization. PMID: 22910359 Findings suggest that transcription factor A (TFAM) is absolutely required to recruit the transcription machinery during initiation of transcription. PMID: 23012404 The expression of TFAM protein was not significantly reduced in ClpX-knockdown cells. PMID: 22841477 Recombinant TFAM increased mitochondrial DNA and abolished the activation of nuclear factor of activated T cells (NFAT), which is well known to activate pathological hypertrophy. PMID: 22709542 study demonstrates that mtDNA damage is involved in liver damage in extrahepatic cholestatic patients. The mtDNA damage is attributable to the loss of TFAM PMID: 22306509 Plasmacytoid dendritic cells (pDC) contribute to sterile immune responses by recognizing the mitochondrial component of necrotic cells (TFAM), with TFAM and mitochondrial DNA as likely mediators of pDC activation. PMID: 22675199

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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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