Recombinant Human Prolyl Endopeptidase Fap (FAP) Protein (His)

Name: Recombinant Human Prolyl Endopeptidase Fap (FAP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00371P
Price: 240.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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100ug

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Product Overview

Description	Recombinant Human Prolyl Endopeptidase Fap (FAP) 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	Q12884
Target Symbol	FAP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	LRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD
Expression Range	26-760aa
Protein Length	Partial
Mol. Weight	86.5 kDa
Research Area	Cancer
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	Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.
Subcellular Location	[Prolyl endopeptidase FAP]: Cell surface. Cell membrane; Single-pass type II membrane protein. Cell projection, lamellipodium membrane; Single-pass type II membrane protein. Cell projection, invadopodium membrane; Single-pass type II membrane protein. Cell projection, ruffle membrane; Single-pass type II membrane protein. Membrane; Single-pass type II membrane protein.; [Antiplasmin-cleaving enzyme FAP, soluble form]: Secreted.; [Isoform 2]: Cytoplasm.
Protein Families	Peptidase S9B family
Database References	HGNC: 3590 OMIM: 600403 KEGG: hsa:2191 STRING: 9606.ENSP00000188790 UniGene: PMID: 30383930 In this study, authors confirm that FAPalpha can promote the generation of Tregs and TAMs, which suggests that FAPalpha plays a immunosuppressive role in the tumor microenvironment PMID: 29273462 Mounting evidence supported that miR-30a-5p directly targetted FAP and suppressed its expression in oral cavity cancer cells (OSCCs). By suppressing FAP expression, miR-30a-5p significantly inhibited cell propagation, migration, and invasion. Therefore, miR-30a-5p might be a new therapeutic target for oral cancer treatment. PMID: 29026005 These results revealed that FAPalpha promoted the growth, adhesion and migration of lung squamous cell carcinoma cells. In addition, FAPalpha regulated lung cancer cell function, potentially via the PI3K and SHH pathways. Further investigations are required to examine the role of FAPalpha in lung AC cells. PMID: 29115573 Several isoforms of DPP-IV and FAP are present in glioblastoma tissue. The absence of alkaline isoforms of both enzymes in glioma cell lines however suggests that isoforms from other, most likely stromal, cell types contribute to the overall pattern seen in glioblastoma tissues. PMID: 28452380 These results indicated that the low plasma FAPalpha level might due to the systemic reaction to the presence of tumor and circulating FAPalpha level might be a potential indicator for diagnosing ESCC. PMID: 28415791 The predictors for FAP occurrence among desmoid tumor patients are large tumor size, intra-abdominal location, multiple tumors, and patient's young age. PMID: 28570749 This evidence highly suggested that FAP is a potential prognosticator of GC patients and a target for synergizing with other treatments, especially immune checkpoint blockades in GC. PMID: 27983931 Mutations to predicted TM interfacial residues (G10L, S14L, and A18L) comprising a small-X3-small motif reduced FAP TM-CYTO dimerization relative to wild type. Predicted off-interface residues showed no significant change from wild type. The interfacial TM residue G10L decreased FAP endopeptidase activity more than 25%, and reduced cell-surface versus intracellular expression relative to interfacial S14L and A18L. PMID: 27155568 proCOL11A1, fibroblast-activated protein, secreted protein acidic and rich in cysteine, and periostin expression was significantly increased in the intratumoral stroma of pancreatic ductal adenocarcinomas compared to paired non-neoplastic pancreata PMID: 29025374 Circulating FAP activity and antigen levels correlate strongly when measured in liver disease and coronary heart disease. PMID: 28582421 Fibroblast activation protein (P=.00117) was stronger than grade and stage in predicting clinical aggressiveness in clear cell renal cell carcinoma. PMID: 27063470 expression of FAP in primary tumors and in their metastases was associated both with synchronous metastases and also with metastases to the lymph nodes PMID: 28033421 have identified fibroblast activation protein (FAP) as the endopeptidase responsible for this site-specific cleavage of human FGF21 (hFGF21), and propose that inhibition of FAP may be a therapeutic strategy to increase endogenous levels of active FGF21. PMID: 27118870 DPP4 activity and/or structure homologue (DASH) proteins are involved in many pathophysiological processes and have therefore been proposed for potential biomarkers or even drug targets in various cancers (DPP4 and FAP). (Review) PMID: 26671446 FAP expression is significantly upregulated in human masticatory mucosa during wound healing PMID: 28005267 Expression of FAPalpha in stroma was associated with distant metastasis of breast phyllodes tumor. PMID: 27881889 High FAPalpha expression is associated with glioblastoma. PMID: 27492457 Increased FAPalpha expression is associated with thyroid papillary carcinoma. PMID: 26715280 The level of FAP expression in NGP-127, SJCRH30, and SJSA-1 lines as well as in cancer-associated fibroblasts of patients was comparable, which makes these cell lines a possible model for studying FAP PMID: 27817025 NPY is efficiently cleaved by FAP indicating a potential function for FAP in neuropeptide regulation within liver and cancer biology. PMID: 26621486 degradomic study highlights cell-contextual proteolysis by FAPalpha with distinct positional profiles. Generally, our findings link FAPalpha to key aspects of CAF biology and attribute an important role in tumor-stroma interaction to FAPalpha PMID: 26304112 Data suggest that a DNA vaccine targeting human fibroblast activation protein alpha (FAPalpha) may be an attractive and effective cancer immunotherapy strategy. PMID: 27020681 In this study, we show for the first time the expression of FAP in activated fibroblasts after MI and its activation by TGFbeta1. Effects of FAP on fibroblast migration and gelatinolytic activity indicate a potential role in cardiac wound healing PMID: 26319660 the circulating protease, fibroblast activation protein, is the proteolytic enzyme responsible for hFGF21 inactivation. PMID: 26635356 FAP is expressed by activated, collagen-synthesizing fibroblasts, but not by inactive fibroblasts or fully differentiated myofibroblasts and non-fibroblast cells in the infarct. PMID: 26454160 This study identified fibroblast activation protein (FAP) as the enzyme that cleaves and inactivates human FGF21. PMID: 26797127 Human FGF-21 Is a Substrate of Fibroblast Activation Protein. PMID: 26962859 FAP selectively cleaves type I collagen resulting in increased macrophage adhesion. PMID: 26934296 FAP sensitizes fibrosarcoma to chemotherapy and alters cell death. PMID: 26342814 Data show that FAP and DPP4 proteins were simultaneously induced in dedifferentiating mature adipocytes supporting a potential role for these enzymes in adipose tissue remodeling and cell plasticity. PMID: 25816202 FAP expression is associated with worse prognosis in solid tumors PMID: 25775399 Deficiency of FAP promoted proteoglycan loss and cartilage degradation in chronic inflammatory arthritis. PMID: 25600705 Demonstrate co-expression of FAP and DPP-IV in pancreatic alpha cells in adult humans. PMID: 25361590 Expression of CCN2, EMA, and FAP may be involved in the activation of cancer associated fibroblasts in hepatocellular carcinoma. PMID: 25126747 Immunofluorescence optical sectioning microscopy of FAPalpha and lipid raft markers further corroborates recruitment of FAPalpha to lipid rafts and invadopodia. PMID: 26209915 High FAP expression is associated with increased metastasis. PMID: 25995078 Soluble fibroblast activation protein plasma levels were reduced in coronary heart disease. PMID: 25464232 Expression of TGF-beta1 is positively related with FAP-alpha expression in primary breast tumors. PMID: 25744843 knockdown of FAP inactivated PTEN/PI3K/AKT and Ras-ERK and its downstream signaling regulating proliferation, migration, and invasion in oral squamous cell carcinoma cells. PMID: 24722280 substrate repertoire and expression patterns of FAP PMID: 24470260 An association was made with circulating levels of FAPalpha and prognosis in acute coronary syndrome. PMID: 23932048 In vitro, FAP-alpha promotes proliferation and inhibits migration of breast cancer cells, potentially by regulating the FAK pathway. PMID: 24885257 The study emphasized FAP as a marker for cutaneous epithelial malignancy and confirmed its diagnostic usefulness in the distinction of Basal cell carcinoma from Trichoepithelioma, and Squamous cell carcinoma from Pseudoepitheliomatous hyperplasia PMID: 24595644 A positive correlation between the expression of FAP-alpha and DPPIV and the activity of both gelatinases was found. PMID: 24789592 IHC revealed protein expression of all four genes. IHC staining for ADAM12, FAP, and WISP1 correlated with CDR and was higher, whereas SOX11 staining was lower in tumors with earlier recurrence following excision PMID: 24402778 FAP is essential for the migration of bone marrow mesenchymal stem cells through RhoA activation. PMID: 24551161 We found that seprase is transcriptionally up-regulated in invasive melanoma cells via the canonical TGF-beta signaling pathway, supporting the roles of both TGF-beta and seprase in tumor invasion and metastasis. PMID: 24727589 C1088T variant in fibroblast activation protein is associated with ER stress, loss of enzymatic function and loss of cell surface localisation. PMID: 24717288 results suggested that FAPalpha might directly promote tumor growth and invasiveness in ovarian cancer cells PMID: 24028972

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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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