FHIT Antibody (YA2677)
(Synonyms: AP3A hydrolase; AP3Aase; Dinucleosidetriphosphatase; FRA3B)FHIT Antibody (YA2677) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to FHIT.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB
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Reactivity :
Human, Rat
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Formulation:
Supplied in rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:500-1:1000 |
Product Details
FHIT Antibody (YA2677) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to FHIT.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Rat
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Observed Molecular WeightObserved band size: 17 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 17 kDa
A synthesized peptide derived from human FHIT aa1-85/147.
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
The FHIT (Fragile Histidine Triad) gene functions as a tumor suppressor, mediating DNA damage response and apoptosis in epithelial cells[1]. Mechanistically, FHIT interacts with multiple signaling pathways, including the ATR/Chk1 axis, to regulate cell cycle checkpoints and maintain genomic stability[2][3]. In disease models, loss of FHIT expression is associated with increased susceptibility to carcinogenesis, particularly in lung, esophageal, and gastrointestinal cancers[4][5]. Compared with related tumor suppressors, FHIT uniquely localizes at common fragile sites and is frequently inactivated by genomic deletions, distinguishing it from isoforms such as WWOX or VHL[6][7]. FHIT deficiency promotes accumulation of DNA lesions and genomic instability, facilitating early oncogenic transformation and progression in epithelial tissues[8]. Experimental studies have employed FHIT restoration and FHIT-mimetic peptides to suppress tumor growth, indicating potential applications for therapeutic intervention[9][10]. These interventions provide a model to study apoptosis induction, replication stress response, and drug sensitivity in FHIT-deficient tumors[9][11]. Therefore, FHIT serves as both a biomarker of genomic instability and a functional target for preclinical studies, enabling mechanistic insights into tumor suppressor pathways and informing the development of precision oncology strategies[12][13].
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Subcellular Localization
Cytoplasm; Mitochondrion; Nucleus
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Expression
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 -
Subunit
Homodimer. Interacts with UBE2I. Interacts with MDM2. Interacts with CTNNB1. Identified in a complex with CTNNB1 and LEF1
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SwissProt ID
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Synonyms
AP3A hydrolase; AP3Aase; Dinucleosidetriphosphatase; FRA3B
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Research Field
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Documentation
[1]. Iida M, et al. Candidate biomarkers for cervical cancer treatment: Potential for clinical practice (Review). Mol Clin Oncol. 2014 Sep;2(5):647-655. [Content Brief]
[2]. Fang JY, et al. Alteration of DNA methylation in gastrointestinal carcinogenesis. J Gastroenterol Hepatol. 2001 Sep;16(9):960-8. [Content Brief]
[3]. Koppert LB, et al. The molecular biology of esophageal adenocarcinoma. J Surg Oncol. 2005 Dec 1;92(3):169-90. [Content Brief]
[4]. Dacic S. Molecular profiling of lung carcinoma: identifying clinically useful tumor markers for diagnosis and prognosis. Expert Rev Mol Diagn. 2007 Jan;7(1):77-86. doi: 10.1586/14737159.7.1.77. PMID: 17187486. et al. Molecular profiling of lung carcinoma: identifying clinically useful tumor markers for diagnosis and prognosis. Expert Rev Mol Diagn. 2007 Jan;7(1):77-86. [Content Brief]
[5]. Fong KM, et al. Lung cancer. 9 [Content Brief]
[8]. Schrump DS, et al. Targets for molecular intervention in multistep pulmonary carcinogenesis. World J Surg. 2001 Feb;25(2):174-83. [Content Brief]
[9]. Wang C, et al. Reviewing once more the c-myc and Ras collaboration: converging at the cyclin D1-CDK4 complex and challenging basic concepts of cancer biology. Cell Cycle. 2011 Jan 1;10(1):57-67. [Content Brief]
[10]. Ray KC, et al. Heparin-binding epidermal growth factor-like growth factor eliminates constraints on activated Kras to promote rapid onset of pancreatic neoplasia. Oncogene. 2014 Feb 13;33(7):823-31. [Content Brief]
[11]. Danesi R, et al. Pharmacogenetics of anticancer drug sensitivity in non-small cell lung cancer. Pharmacol Rev. 2003 Mar;55(1):57-103. [Content Brief]
[12]. Basu A, et al. Genes related to estrogen action in reproduction and breast cancer. Front Biosci. 2005 Sep 1;10:2346-72. [Content Brief]
[13]. Radhakrishnan R, et al. DNA hypermethylation as an epigenetic mark for oral cancer diagnosis. J Oral Pathol Med. 2011 Oct;40(9):665-76. [Content Brief]
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