Recombinant Human Hepatocyte Nuclear Factor 3-Alpha (FOXA1) Protein (His&Myc)

Name: Recombinant Human Hepatocyte Nuclear Factor 3-Alpha (FOXA1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01925P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Hepatocyte Nuclear Factor 3-Alpha (FOXA1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P55317
Target Symbol	FOXA1
Synonyms	Forkhead box protein A1 (Transcription factor 3A) (TCF-3A)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MLGTVKMEGHETSDWNSYYADTQEAYSSVPVSNMNSGLGSMNSMNTYMTMNTMTTSGNMTPASFNMSYANPGLGAGLSPGAVAGMPGGSAGAMNSMTAAGVTAMGTALSPSGMGAMGAQQAASMNGLGPYAAAMNPCMSPMAYAPSNLGRSRAGGGGDAKTFKRSYPHAKPPYSYISLITMAIQQAPSKMLTLSEIYQWIMDLFPYYRQNQQRWQNSIRHSLSFNDCFVKVARSPDKPGKGSYWTLHPDSGNMFENGCYLRRQKRFKCEKQPGAGGGGGSGSGGSGAKGGPESRKDPSGASNPSADSPLHRGVHGKTGQLEGAPAPGPAASPQTLDHSGATATGGASELKTPASSTAPPISSGPGALASVPASHPAHGLAPHESQLHLKGDPHYSFNHPFSINNLMSSSEQQHKLDFKAYEQALQYSPYGSTLPASLPLGSASVTTRSPIEPSALEPAYYQGVYSRPVLNTS
Expression Range	1-472aa
Protein Length	Full Length
Mol. Weight	56.6 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	Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3'. Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Its differential recruitment to chromatin is dependent on distribution of histone H3 methylated at 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the development of multiple endoderm-derived organ systems such as liver, pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles. Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription; required for ESR1 binding to the NKX2-1 promoter in breast cancer cells; binds to the RPRM promoter and is required for the estrogen-induced repression of RPRM. Involved in regulation of apoptosis by inhibiting the expression of BCL2. Involved in cell cycle regulation by activating expression of CDKN1B, alone or in conjunction with BRCA1. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis.
Subcellular Location	Nucleus.
Database References	HGNC: 5021 OMIM: 602294 KEGG: hsa:3169 STRING: 9606.ENSP00000250448 UniGene: PMID: 30066917 FoxA1 might be related to the development and differentiation of secretory coil-like structures, as well as the secretory function of the 3D reconstructed eccrine sweat glands. PMID: 29909922 TUG1 promoted osteosarcoma cell proliferation and suppressed apoptosis by regulating the miR-212-3p/FOXA1 axis. PMID: 29793327 miR-760 should be considered as a tumor suppressor since it negatively regulates the oncogene protein FOXA1 and regulated TRAIL sensitivity in Non-small cell lung cancer cells. PMID: 29665655 As a tumor suppressor, FOXA1 targets PIK3R1 directly to inhibit PI3K/Akt signaling pathway, thus exerting a negative regulatory effect on proliferation, migration, and invasion of HCC in male patients. PMID: 29208003 miR212 suppresses renal cell carcinoma (RCC) proliferation and invasion by modulating FOXA1, suggesting that miR212 may have potential as a therapeutic target in RCC. PMID: 29115609 the results of the present study suggested that FOXA1 is a potential oncogene in NSCLC PMID: 29115441 During the ensuing weeks, the PAX2/FOXA1 boundary progressively extended cranially such that by 21 weeks the entire vaginal epithelium was FOXA1-reactive and PAX2-negative. This observation supports Bulmer's proposal that human vaginal epithelium derives solely from urogenital sinus epithelium PMID: 28918284 The transcription factor FOXA1 directly bound to the PLOD2 promoter, and turned on PLOD2 transcription. In summary, our findings revealed a regulatory mechanism of NSCLC metastasis through EGFR-PI3K/AKT-FOXA1-PLOD2 pathway. PMID: 29072684 maintenance of the cancer cell state is dependent on recruitment of Mediator and Cohesin through FOXA and master transcription factors PMID: 27739523 overexpression of GATA3 and FOXA1 cooperate with PPAR activation to drive transdifferentiation of a basal bladder cancer cells to a luminial phenotype. PMID: 27924948 Results found FOXA1 to be hypermethylated in breast tumors from African American (AA) versus European American (EA) women with ER- cancer, and methylation levels showed strong inverse relationships with both mRNA and protein levels. A significant positive association was identified between parity and FOXA1 methylation in tumors from AA women who did not breastfeed. PMID: 28756535 High expression of FOXA1 is associated with breast tumor. PMID: 28534958 High FOXA1 expression was significantly associated with presence of lymph node metastasis (LNM), low tumour-infiltrating lymphocytes (TILs), and submucosal invasion. PMID: 28843920 Results provide evidence that the atypical expression of FOXA1 transcriptional factor is an important player in psoriasis, as it inhibits maturation of naive T cells into a Treg subpopulation, therefore contributing to the development of psoriatic skin lesions. PMID: 28849568 Authors demonstrated that ER(alpha), GATA3 and FOXA1 form a transcriptional complex with Ell3 to regulate IL-20 expression in ER(+) breast cancer cells. FOXA1 represses IL-20 expression, whereas GATA3 and ER(alpha) activate it. PMID: 28514748 the findings show that squamous and micropapillary bladder cancers have different expression patterns of CK14 and FOXA1 and suggest that they arise from distinct precursors. PMID: 28721490 rs4442975 may not confer a risk of breast cancer occurrence or progression in the Chinese Han population. PMID: 27835577 As a transcriptionally regulated program, urothelial differentiation operates as a heterarchy, wherein GATA3 is able to co-operate with FOXA1 to drive expression of luminal marker genes, but that P63 has potential to transrepress expression of the same genes. PMID: 28282036 FOXA1 overexpression mediates endocrine resistance by altering the ER transcriptome and IL-8 expression in ER-positive breast cancer. PMID: 27791031 Findings suggested FOXA1 may act as an anti-oncogene in gastric cancer (GC) cells. Low-level expression of FOXA1 protein was confirmed in GC tissues and cell lines. FOXA1 over-expression could significantly affect cell proliferation, apoptosis and tumor invasion of GC cells, which may be resulted by reversing EMT. PMID: 29129808 High expression of FOXA1 is an independent prognostic parameter in ERG negative prostate cancer PMID: 29029032 A molecular mechanism by which Estradiol antagonizes GR-dependent induction of specific genes by preventing the recruitment of the pioneer factors FOXA1 and FOXA2 in a physiologically relevant model. PMID: 28938408 Results show that c-Abl phosphorylates FoxA1 at multiple sites. Tyr429 and Tyr464 were identified as the major phosphorylation sites in the FoxA1 C-terminal region. This c-Abl-mediated phosphorylation of FoxA1 promotes the activation of estrogen signaling by inducing its binding to histones. PMID: 27883218 MLL3 binding was dependent on FOXA1, indicating that FOXA1 recruits MLL3 to chromatin. MLL3 silencing decreased H3K4me1 at enhancer elements but had no appreciable impact on H3K4me3 at enhancer elements. We propose a mechanism whereby the pioneer factor FOXA1 recruits the chromatin modifier MLL3 to facilitate the deposition of H3K4me1 histone marks, subsequently demarcating active enhancer elements PMID: 27926873 FoxA1 discriminates between medullary thyroid carcinoma and tumors of follicular derivation with sensitivity and specificity greater than calcitonin and carcinoembryonic antigen. PMID: 28546130 FOXA1 loss may play a significant role in enabling prostate cancer progression to neuroendocrine prostate cancer, whereas IL-8 and MAPK/ERK pathways may be promising targets for therapeutic intervention. PMID: 28319070 Low FOXA1 expression is associated with breast cancer invasion and metastasis. PMID: 27524420 the distinct mechanisms by which GATA2 and FOXA1 regulate AR cistrome and suggest that FOXA1 acts upstream of GATA2 and AR in determining hormone-dependent gene expression in prostate cancer. PMID: 26751772 Study implicates enhancer reprogramming, FOXA1 upregulation, and a retrograde developmental transition in pancreatic ductal adenocarcinoma metastasis. PMID: 28757253 Studies indicate that microRNA miR-212 exerts its inhibitory effect on hepatocellular carcinoma (HCC) by inhibiting forkhead transcription factor FOXA1 expression. PMID: 27999212 FOXA1 is expressed by basal cells of squamous epithelium, pre-invasion lesions of the uterine cervix and the head/neck and almost half invasive cervical and head/neck carcinomas, supporting its possible implication in HPV associated carcinomas. PMID: 28209524 CREB1/FoxA1 signaling is a targetable driver of prostate cancer progression and serves as a biomarker of poor clinical outcomes. PMID: 26743006 miR-93 may promote the process of epithelial-mesenchymal transition in endometrial carcinoma cells by targeting FOXA1. PMID: 27829043 conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 stability. These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis. PMID: 28455227 FOXA1 is not only able to recognize but also remodel the epigenetic signatures at lineage-specific enhancers, which is mediated, at least in part, by a feed-forward regulatory loop between FOXA1 and TET1. PMID: 27257062 Based on these results, we suggest that FOXA1 plays a catalytic role in ovarian cancer pathogenesis and development by affecting the expression of the above-mentioned proteins. PMID: 28488543 these results suggest that FOXA1 suppresses expression of IL6 through inhibition of NF-kappaB recruitment to the IL6 promoter in an ERalpha-independent manner and that reduction in FOXA1 expression induces IL6 expression and contributes to cancer stem cell-like properties in TAM-R cells. PMID: 28270510 These results suggest a positional-nucleosome-oriented accessing model for Pioneer factors seeking target motifs, in which FOXA1 can examine each underlying DNA nucleotide. PMID: 27458208 Down-regulation of TRPS1 by miR-373, acting as a transcriptional activator, promotes epithelial-mesenchymal transition (EMT) and metastasis by repressing FOXA1 transcription, expanding upon its previously reported role as a transcription repressor. PMID: 26969828 FOXA1 is found in ovarian mucinous and Brenner tumours PMID: 28238418 the results of the present study indicated that FOXA1 may be considered a potential prognostic marker, and may promote tumor growth of CRC by upregulating YAP expression. PMID: 27484093 meta-analysis showed that high expression of FOXA1 in breast cancer patients was a good prognostic indicator for survival outcome. PMID: 27212698 FOXA1 promotes cell senescence in EC by interaction with p16INK4a. PMID: 27349269 There is significantly increased esophageal squamous cell carcinoma risk associated with the FOXA1 rs7144658 T > C polymorphism among male patients. PMID: 27050876 Meta-analysis results clearly point to an important role of FOXA1 and FOXA2 gene regulatory networks in the etiology of Alzheimer's disease PMID: 26890743 show that ER and GR both have the ability to alter the genomic distribution of the FoxA1 pioneer factor. Single-molecule tracking experiments reveal a highly dynamic interaction of FoxA1 with chromatin in vivo; FoxA1 factor is not associated with footprints at its binding sites throughout the genome; findings support a model wherein interactions between transcription factors and pioneer factors are highly dynamic. PMID: 27062924 findings suggest a key role for GalNAc-T4 in the estrogen pathway through FOXA1 glycosylation PMID: 26541755 The ratio of FoxA1 to FoxA2 in lung adenocarcinoma is regulated by LncRNA HOTAIR and chromatin remodeling factor LSH PMID: 26658322 Loss of Interdependent Binding by the FoxO1 and FoxA1/A2 Forkhead Transcription Factors Culminates in Perturbation of Active Chromatin Marks and Binding of Transcriptional Regulators at Insulin-sensitive Genes. PMID: 26929406

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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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