Recombinant Human FHIT Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2088

Recombinant Human FHIT Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2088
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His
Host Species Human
Accession P49789
Synonym AP3Aase, FRA3B
Background Fragile histidine triad, also known as FHIT, may play a key role in differentiating humans from apes. Fragile histidine triad gene belongs to the histidine triad gene family. It has been shown that fragile histidine triad synergizes with VHL, another tumor suppressor, in protecting against chemically - induced lung cancer. Fragile histidine triad gene works as a tumor suppressor as it has been demonstrated in animal studies. The exact molecular function of FHIT is still partially unclear. It also acts as a tumor suppressor of HER2/neu driven breast cancer.
Description A DNA sequence encoding the human FHIT (P49789) (Met1-Gln147) was expressed with a His tag at the C-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met1-Gln147
Molecular Weight The recombinant human FHIT consists of 153 a.a. and predicts a molecular mass of 17.7 KDa. It migrates as an approximately 18 KDa band in SDS-PAGE under reducing conditions.
Purity >85% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 50mM Tris, 10% glycerol, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Possesses dinucleoside triphosphate hydrolase activity. Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate. Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate. Also catalyzes the ammonolysis of adenosine 5-phosphorofluoridate and diadenosine triphosphate. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.
Subcellular Location Cytoplasm. Mitochondrion. Nucleus.
Database References
Associated Diseases A chromosomal aberration involving FHIT has been found in a lymphoblastoid cell line established from a family with renal cell carcinoma and thyroid carcinoma. Translocation t(3;8)(p14.2;q24.1) with RNF139. Although the 3p14.2 breakpoint has been shown to interrupt FHIT in its 5-prime non-coding region, it is unlikely that FHIT is causally related to renal or other malignancies.
Tissue Specificity Low levels expressed in all tissues tested. Phospho-FHIT observed in liver and kidney, but not in brain and lung. Phospho-FHIT undetected in all tested human tumor cell lines.

Gene Functions References

  1. FHIT predicts better clinical relevance for patients with bladder cancer. PMID: 29752880
  2. Fhit expression impacts the translation of a number of cancer associated genes. PMID: 29282095
  3. overexpression of Fhit, a tumor suppressor protein, induces autophagy in NSCLC cells. Further, we found that this autophagy is mediated by 14-3-3tau and plays a cytoprotective role against the antitumor effect of Fhit both in vitro and in vivo. PMID: 28404875
  4. Review/Meta-analysis: significant difference in FHIT gene promoter methylation status in non-small cell lung carcinoma patients was found in Asians but not in Caucasian population. PMID: 28036263
  5. these results show that squamous cell carcinomas of the vulva presents a characteristic molecular pattern with FHIT being downregulated whereas HMGA2 is upregulated PMID: 27835588
  6. It has been proposed that Fhit and Wwox loss work synergistically in cancer progression and that DNA damage caused by Fhit could be targeted early in cancer initiation for prevention, while DNA damage caused by Wwox loss could be targeted later in cancer progression, particularly in cancers that develop resistance to genotoxic therapies. (Review) PMID: 27773744
  7. Two variants were identified for maximal voluntary ventilation and located in the genes of LOC102724340 (rs41434646) and FHIT (rs9833533). FHIT represses transcriptional activity of beta-catenin, a critical protein for growth of skeletal muscle, and thus might have influenced the level of maximal voluntary ventilation. PMID: 29095316
  8. This study demonstrates that Fhit down-regulation is an early event in both multistep carcinogenic processes leading to pancreatic ductal adenocarcinoma PMID: 28289900
  9. The results have implications for the mechanism by which Fhit regulates TK1 mRNA, and more broadly, for its modulation of multiple functions as tumor suppressor/genome caretaker. PMID: 28093273
  10. RARb and FHIT promoter methylation may be associated with the carcinogenesis of cervical cancer. FHIT promoter methylation may play a crucial role in cervical cancer progression. Additional studies with large sample sizes are essential to confirm our findings. PMID: 28639889
  11. The peptide was located within the 'disordered' region, which is invisible in the known crystal structures of Fhit. PMID: 28094435
  12. Both the 3p14.2 locus copy number and FHIT protein expression levels showed significant decreases when CIN transitioned to cervical cancer. PMID: 28414756
  13. Study indicate that the observed level of FHIT promoter methylation was not enough to suppress gene expression in non-small cell lung cancer (NSCLC). Lack of negative correlation between FHIT expression and methylation, or positive correlation between gene expression and immunoexpression suggest the role of another molecular mechanisms regulating FHIT expression on mRNA and protein levels in NSCLC patients. PMID: 27572663
  14. High methylation in the FHIT promoter region is associated with lung cancer. PMID: 27716889
  15. the expression profile of miRNAs that may be associated with expression of the FHIT gene in breast cancer, was examined. PMID: 27236032
  16. FHIT hypermethylation, which induces the inactivation of FHIT gene, plays an important role in the carcinogenesis and clinical outcome and may serve as a potential drug target of non-small cell lung cancer. PMID: 26796853
  17. FHIT hypermethylation, which induces the inactivation of FHIT gene, plays an important role in the carcinogenesis and clinical outcome and may serve as a potential diagnostic marker and drug target of non-small-cell lung carcinoma PMID: 26929601
  18. Low FHIT Gene Expression is associated with Acute Lymphoblastic Leukemia. PMID: 26745060
  19. In 22 lung cancer patients with negative histology and cytology at initial bronchoscopy, FHIT and p16 mRNA loss was detected in 40.9% (9/22) and 36.4% (8/22) cases, respectively. PMID: 23709347
  20. The results showed that the methylation levels of both BRCA1 and FHIT promoters were higher in the serum of the breast ductal carcinoma group than those of the breast fibroadenoma group. PMID: 26406001
  21. Review/Meta-analysis: FHIT methylation could be a diagnostic biomarker of breast carcinogenesis. PMID: 26491255
  22. Mutations of the FHIT gene are not major cause of Peutz-Jeghers syndrome. PMID: 27060312
  23. Adenylylsulfate-ammonia adenylyltransferase activity is another inherent property of Fhit proteins. PMID: 26181368
  24. APOBEC3B overexpression and Fhit-loss induced DNA damage are independent events that, when occurring together, result in a significantly increased frequency of APOBEC-induced mutations that drive cancer progression. PMID: 25401976
  25. Hypermethylation of FHIT gene is associated with Epstein-Barr virus-associated gastric carcinomas. PMID: 25720522
  26. FHIT promotor hypermethylation is associated with the development of breast cancer. PMID: 25735361
  27. Data indicate that fragile histidine triad protein [FHIT) contributes partially to radioresistance and predicts clinical outcomes in irradiated oral cancer. PMID: 25460508
  28. Fhit nuclear translocation upon mitogenic stimulation may represent a new regulatory mechanism that allows rapid restoration of Fhit cytoplasmic levels and promotes the proliferation cascade activated by mitogenic stimulation PMID: 25711523
  29. Data are consistent with a mechanism in which Fhit protein is required for accumulation of the transcriptional repressor of HMOX1, Bach1 protein. PMID: 25486479
  30. the decrease in the expression of miR-29b by c-Myc may be responsible for FHIT loss-mediated tumor aggressiveness and for poor outcome in non-small cell lung cancer. PMID: 24909176
  31. the induction of Slug expression by AKT/NF-kappaB signaling pathway due to FHIT loss not only promotes tumor invasion, but also confers cisplatin resistance due to Slug-mediated PUMA reduction in lung cancer cells. PMID: 24998847
  32. Patients with FHIT methylation might promote cervical cancer progression. PMID: 25422218
  33. we demonstrate that the expression pattern of FHIT and miR-30c is inversely correlated with that of MTDH and HMGA2 in normal tissue, non-metastatic and metastatic tumors, serving as a potential biomarker for metastasis in lung cancer. PMID: 25340791
  34. The Fhit possesses diadenosine triphosphate hydrolase activity, but although reduction of its enzymatic activity appears to be important for exerting its tumor suppressor function, the regulation of Fhit activity is poorly understood. PMID: 25098403
  35. methylation of FHIT is a useful biomarker of biologically aggressive disease in patients with non-small cell lung carcinomas PMID: 24935385
  36. The total frequency of FHIT, RASSF1A and RARbeta gene methylation was significantly higher in lung cancer. PMID: 25040980
  37. Hypermethylation of FHIT gene promoter region was found more frequent in cancer tissue than controls. PMID: 24667261
  38. FHIT expression can block the PI3K-Akt pathway by suppressing phosphorylation of Akt in cholangiocarcinoma cells. PMID: 24757411
  39. Loss of FHIT function leads to nucleotide imbalance, spontaneous replication stress, and DNA breaks. [review] PMID: 25283145
  40. FHIT loss was observed in 64% of non-small-cell lung carcinoma patients and was significantly associated with squamous cell carcinoma and poor tumor grade. PMID: 24185125
  41. These results showed that Fhit was up-regulated specifically by activating Galpha subunits of the Gq subfamily but not by those of the other G protein subfamilies. PMID: 23993961
  42. The expressions of DAPK1, FHIT, MGMT, and CDKN2A were detected The methylation of the promoter region significantly decreased the expression of only DAPK1 PMID: 23494221
  43. our meta-analysis provides evidences that negative expression of FHIT protein may be correlated with poor prognosis in patients with gastric cancer PMID: 24729090
  44. Fhit delocalizes annexin A4 from plasma membrane to cytosol and sensitizes lung cancer cells to paclitaxel. PMID: 24223161
  45. Results identify a novel member of the miR-548 family in the fourth intron of the human FHIT gene. PMID: 24556720
  46. Data indicate that expression of several predicted chimeric genes and genes with disrupted exon structure including ALK, NBAS, FHIT, PTPRD and ODZ4 in neuroblastoma. PMID: 23991058
  47. Immunohistochemical staining of oral squamous cell carcinoma shows that Fhit negativity is associated with cervical lymph node metastasis and poor disease-specific survival. PMID: 23944951
  48. Our results suggest that loss of Fhit expression in breast cancer is associated with poor prognostic features, and it is also relevant to the results in HER2-negative breast cancer. PMID: 23969757
  49. Reduced expression of FHIT gene is associated with the progression of colon adenocarcinoma. PMID: 24370550
  50. FHIT gene is a "caretaker gene" necessary for maintenance of genome stability. PMID: 23929738


Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed