Recombinant Human Fatty Acid Synthase (FASN) Protein (His)

Name: Recombinant Human Fatty Acid Synthase (FASN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03559P
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 Fatty Acid Synthase (FASN) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P49327
Target Symbol	FASN
Synonyms	[Acyl-carrier-protein] S acetyltransferase; [Acyl-carrier-protein] S malonyltransferase; 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase; 3-oxoacyl-[acyl-carrier-protein] reductase; 3-oxoacyl-[acyl-carrier-protein] synthase; Enoyl-[acyl-carrier-protein] reductase; FAS; FAS_HUMAN; FASN; Fatty acid synthase; MGC14367; MGC15706; OA 519; Oleoyl-[acyl-carrier-protein] hydrolase; SDR27X1; Short chain dehydrogenase/reductase family 27X member 1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIIS
Expression Range	2155-2495aa
Protein Length	Partial
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.
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	Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.
Subcellular Location	Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Database References	HGNC: 3594 OMIM: 600212 KEGG: hsa:2194 STRING: 9606.ENSP00000304592 UniGene: PMID: 29453645 FASN-induced S6 kinase facilitates USP11-eIF4B complex formation for sustained oncogenic translation in diffuse large B-cell lymphoma. PMID: 29483509 HIV-1 infection increases intracellular levels of fatty acid synthase (FASN). Despite the requirement of FASN for nascent virion production, FASN activity was not required for intracellular Gag protein production, indicating that FASN dependent de novo fatty acid biosynthesis contributes to a late step of HIV-1 replication PMID: 28962653 Findings showed that FASN is upregulated in colorectal cancer cell lines that overexpress PGC-1alpha and indicated that FASN expression may enhance cancer cell proliferation by regulating antioxidant enzyme production and resistance to ROS-induced apoptosis. Further data provided evidence that FASN expression was regulated indirectly by PGC-1alpha. PMID: 29130104 Repression of FAS mRNA expression is the consequence of feedback inhibition of FAS expression by long chain fatty acyl-CoAs, which are formed by FACL3 during its upregulation by vitamin D3 in prostate cancer cells. PMID: 15556626 analysis of the expression of fatty acid synthase, Ki-67 and p53 in squamous cell carcinomas of the larynx PMID: 18949744 Fatty acid synthase (FASN) mRNA and protein overexpression were associated with unfavorable clinicopathologic factors and poor outcomes. PMID: 28442505 KRAS is associated with activation of ERK2, induction of FASN, and promotion of lipogenesis. PMID: 28400509 The study has shown that the high frequency of FASN expression in intraepithelial neoplasia (hPIN)and cancer and no expression in most structures of benign hyperplasia make it possible to use this protein as an additional marker in the differential diagnosis of prostatic neoplasms. PMID: 28418352 FASN inhibition/knockdown significantly increased the susceptibility of cisplatin-resistant cells to NK cell cytotoxicity. PMID: 29306075 FASN has a role in leucine deprivation-inhibited proliferation and apoptosis of human breast cancer cells PMID: 27579768 HER2-FASN lipogenic axis delineates a group of breast cancer patients that might benefit from treatment with therapeutic regimens containing FASN inhibitors PMID: 27714708 FASN expression is down-regulated by miR-15a and miR-16-1 in breast cancer cells, regulating cell proliferation. PMID: 27713175 These findings implicate Spot14 as a direct protein enhancer of FASN catalysis in the mammary gland during lactation when maximal MCFA production is needed. PMID: 24771867 High FASN expression is associated with prostate cancer growth. PMID: 26934656 We show that elevated levels of PPARG strongly correlate with elevation of FASN in human prostate cancer (CaP) and that high levels of PPARG/FASN and PI3K/pAKT pathway activation confer a poor prognosis.These data suggest that CaP patients could be stratified in terms of PPARG/FASN and PTEN levels to identify patients with aggressive CaP who may respond favorably to PPARG/FASN inhibition. PMID: 27357679 High FASN expression is associated with meningioma and schwannoma. PMID: 28729415 our findings show that microRNA-195 inhibits pancreatic cancer cell proliferation and invasion by regulating the fatty acid synthase/Wnt signaling pathway, suggesting a tumor suppressive role for microRNA-195 in the development and progression of pancreatic cancer. Thus, inhibiting fatty acid synthase by microRNA-195 may serve as a novel therapeutic approach for the treatment of pancreatic cancer. PMID: 28639885 Inhibition of FASN can decrease the levels of IGFBP1, and the expression, activity, and ubiquitination of HIF-1alpha. Inhibition of FASN can suppress migration, invasion and healing of hepatoma carcinoma cells by decreasing HIF-1alpha, and IGFBP1. PMID: 28197637 The involvement of SREBP-1c and ChREBP in FASN promoter histone modification.Histone acetylation affects FASN transcription by influencing ChREBP-binding carbohydrate-responsive elements. PMID: 28027934 Fatty acid synthase (FASN) inhibitors reduce proliferation and promote apoptosis in high FASN producers lymphatic endothelial cells (HDLEC) cells. PMID: 27918556 MACC1 and FASN are positively correlated and responsible for the poor prognoses in gastric cancer patients.FASN role in gastric cancer resistance to oxaliplatin. PMID: 28339092 Fatty acid synthase fine-tunes the cell's response to stress and injury by remodeling cellular O-GlcNAcylation PMID: 28232487 B7-H3 hijacks SREBP-1/FASN signaling mediating abnormal lipid metabolism in lung cancer PMID: 27939887 Uterine leiomyomata risk was positively associated with FASN AA genotype of SNP rs4247357 among the 7% of African American women with >40% European ancestry. PMID: 27375065 DNA methylation in HIF3A shares moderate correlation between adipose tissue and blood, and both are associated with BMI. In contrast, methylation in FASN is poorly correlated across tissues, but the DNA methylation in adipose tissue but not blood is highly associated with BMI PMID: 26891033 the present study provided evidence that miR320 may directly target fatty acid synthase. These results suggest that miR320 may serve as a therapeutic biomarker of NSCLC in the future. PMID: 27277534 increased expression of NF-YA may promote a malignant phenotype in OS cells via modulation of FASN expression. PMID: 27840951 Results suggest investigation of combined fatty acid synthase (FASN) inhibition and taxane treatment as a therapy for a variety of cancers. PMID: 28159572 our study suggests that miR12075p/FASN plays an important role in hepatocellular carcinoma PMID: 27461404 Our observations suggest a physiological role of placental FASN in human pregnancy. Future studies will clarify whether circulating FASN of placental origin does actually regulate placental and fetal growth PMID: 27090298 Results suggest that FASN plays a pivotal role in glioma neovascularization, and inhibition of FASN may be a potential target for anti-angiogenic therapy for glioma. PMID: 27601165 The role of FASN in breast cancer [review] PMID: 26951539 FASN, ErbB2-high-expressing SK-BR-3 cells displayed higher levels of glycolysis and migration than FASN, ErbB2-low-expressing MCF7 cells. PMID: 26936618 S-nitrosylation of FAS at normal physiological levels of NO increases its activity through dimerization and may contribute to the proper regulation of adipogenesis PMID: 26851298 concluded that EGFR can be activated intracellularly by FASN-dependent palmitoylation PMID: 26378037 Our results suggest that FASN upregulation and PTEN downregualtion may be involved in peritoneal dissemination for gastric cancer progression. PMID: 26514456 Data suggest that thioesterase 2 (TE2) catalytic domain of FASN exhibits novel capping domain insert within the alpha/beta hydrolase core; TE2 (as opposed to TE1 domain) readily releases short chain fatty acids from full-length FASN during turnover. PMID: 26663084 data demonstrate that selective and potent FASN inhibition with TVB-3166 leads to selective death of tumor cells, without significant effect on normal cells, and inhibits in vivo xenograft tumor growth at well-tolerated doses. PMID: 26425687 Results showed correlated FASN regulation relative to key signaling genes with tumor invasion and differentiation in primary retinoblastoma (RB) tissues. Its silencing exerted definite anti-cancer effects in RB cells through PI3K/AKT signaling pathway. PMID: 25958981 Findings indicate that overexpression of FASN plays a crucial role in maintaining energy homeostasis in CRC via increased oxidation of endogenously synthesized lipids. PMID: 25970773 TG levels are regulated by HCBP6-sterol regulatory element binding protein 1c (SREBP1c)-mediated fatty acid synthase (FASN) expression. PMID: 25855506 Loss of fatty acid synthase suppresses the malignant phenotype of colorectal cancer cells by down-regulating energy metabolism and mTOR signaling pathway. PMID: 26109148 In the present study it was determined whether three key enzymes for glycolysis, glutaminolysis and de novo synthesis of FAs, hexokinase-2, glutaminase and fatty acid synthase PMID: 26134042 FASN and HER2 have roles in breast cancer and are blocked by EGCG with pertuzumab or temsirolimus PMID: 26107737 Overall, no SNPs were associated with any known aggressiveness indicators. FASN staining intensity was stronger in malignant than in benign tissue, and NADT was associated with decreased FASN staining in both benign and malignant tissue PMID: 25868764 The results suggested that differential levels of P-glycoprotein, Caveolin-1 and Fatty acid synthase except CYP450 play a major role in acquired resistant phenotype in bladder cancer. PMID: 26025399 FASN inhibition induced apoptosis in chemosensitive and platinum-resistant ovarian cancer cells and may reverse cisplatin resistance. PMID: 25947066 These results for the first time indicated that a cross talk in FASN and HER2 expressions might be associated with prognosis in malignant ovarian cancer. PMID: 25433947 The results reveal that the cytotoxic effects of FASN inhibitors in sensitive lines may be due to the robust depletion of oncogenic signaling lipids, such as diacylglycerols and the elevation of tumor-suppressing ceramides. PMID: 25871544

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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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