Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

FAP

Uniprot No.

Q12884

Research Area

Cancer

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

26-760aa

Target Protein Sequence

LRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

86.5 kDa

Protein Length

Partial

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The Recombinant human Prolyl endopeptidase FAP is produced in E. coli and exhibits a purity exceeding 85%, confirmed by SDS-PAGE analysis. This partial-length protein, spanning the 26-760aa region, is tagged with an N-terminal 6xHis-tag, enhancing its utility in research applications. This recombinant FAP is available in either liquid form or as a lyophilized powder, offering flexibility in experimental design.

FAP exhibits robust endopeptidase activity, cleaving peptide bonds within proteins, while its dipeptidyl peptidase activity is relatively weak [1]. This dual functionality allows FAP to participate in various biological processes, such as the activation of growth factors and the modulation of inflammatory responses [2][3].

FAP is predominantly expressed in the reactive stroma of tumors, making it an attractive target for cancer therapies. Its expression is upregulated in various cancers, including breast, colorectal, and pancreatic cancers, where it is associated with tumor progression and metastasis [4][5]. FAP not only contributes to the degradation of extracellular matrix components but also influences the behavior of fibroblasts and other stromal cells, thereby facilitating tumor growth and invasion [6][7].

References:
[1] C. Huang, C. Suen, C. Lin, C. Chien, H. Lee, K. Chunget al., Cleavage-site specificity of prolyl endopeptidase fap investigated with a full-length protein substrate, The Journal of Biochemistry, vol. 149, no. 6, p. 685-692, 2011. https://doi.org/10.1093/jb/mvr017
[2] D. Dunshee, T. Bainbridge, N. Kljavin, J. Zavala-Solorio, A. Schroeder, R. Chanet al., Fibroblast activation protein cleaves and inactivates fibroblast growth factor 21, Journal of Biological Chemistry, vol. 291, no. 11, p. 5986-5996, 2016. https://doi.org/10.1074/jbc.m115.710582
[3] F. Keane, N. Nadvi, T. Yao, & M. Gorrell, Neuropeptide y, b‐type natriuretic peptide, substance p and peptide yy are novel substrates of fibroblast activation protein‐α, Febs Journal, vol. 278, no. 8, p. 1316-1332, 2011. https://doi.org/10.1111/j.1742-4658.2011.08051.x
[4] A. LeBeau, W. Brennen, S. Aggarwal, & S. Denmeade, Targeting the cancer stroma with a fibroblast activation protein-activated promelittin protoxin, Molecular Cancer Therapeutics, vol. 8, no. 5, p. 1378-1386, 2009. https://doi.org/10.1158/1535-7163.mct-08-1170
[5] K. Lee, K. Jackson, V. Christiansen, C. Lee, J. Chun, & P. McKee, Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein, Blood, vol. 107, no. 4, p. 1397-1404, 2006. https://doi.org/10.1182/blood-2005-08-3452
[6] K. Chung, S. Hsu, Y. Chu, M. Lin, W. Jiaang, R. Chenet al., Fibroblast activation protein (fap) is essential for the migration of bone marrow mesenchymal stem cells through rhoa activation, Plos One, vol. 9, no. 2, p. e88772, 2014. https://doi.org/10.1371/journal.pone.0088772
[7] K. Jackson, V. Christiansen, V. Yadav, R. Silasi‐Mansat, F. Lupu, V. Awasthiet al., Suppression of tumor growth in mice by rationally designed pseudopeptide inhibitors of fibroblast activation protein and prolyl oligopeptidase, Neoplasia, vol. 17, no. 1, p. 43-54, 2015. https://doi.org/10.1016/j.neo.2014.11.002

Target Background

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.

Gene References into Functions

FAP is virtually absent in normal tissues, but it is present in the embryonic and tumor tissues, which makes it a selective and versatile model. In this work, basic approaches to affecting the CAF using FAP as a target were discussed. 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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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

Tissue Specificity

Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from in

Database Links

HGNC: 3590

OMIM: 600403

KEGG: hsa:2191

STRING: 9606.ENSP00000188790

UniGene: Hs.654370

Code	CSB-EP008424HUa0
Abbreviation	Recombinant Human FAP protein, partial
MSDS	MSDS Datasheet
Size	$224
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human Prolyl endopeptidase FAP (FAP), partial

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