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Mouse Fap Antibody(N-term)

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Mouse Fap Antibody(N-term) AP19697a
    All lanes : Anti-Mouse Fap Antibody(N-term) at 1:500 dilution Lane 1: Mouse kidney lysate Lane 2: Mouse ovary lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 88 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 1 - Mouse Fap Antibody(N-term) AP19697a
    Anti-Mouse Fap Antibody(N-term) at 1:2000 dilution + mouse kidney lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 88 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P97321
Other Accession NP_032012.1
Reactivity Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Additional info
Gene ID 14089
Other Names Prolyl endopeptidase FAP, Fap {ECO:0000312|MGI:MGI:109608}
Target/Specificity This Mouse Fap antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 15-41 amino acids from the N-terminal region of mouse Fap.
Dilution WB~~1:2000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsMouse Fap Antibody(N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name Fap {ECO:0000312|MGI:MGI:109608}
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, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also 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.
Cellular Location Prolyl endopeptidase FAP: Cell surface. Cell membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein. Membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein. Note=Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. {ECO:0000250|UniProtKB:Q12884}
Tissue Location Expressed strongly in uterus, pancreas, submaxillary gland and skin, less in lymph node, ovary, skeletal muscle, adrenal and bone marrow. Expressed in reactive stromal fibroblast in epithelial cancers. Expressed in melanocytes but not melanomas (at protein level). Detected in fibroblasts, in placenta, uterus, embryos from day 7-19 and in newborn mice (P1)
Research Areas

BACKGROUND

In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM (By similarity). May have a role in tissue remodeling during development and wound healing, and contribute to invasiveness in malignant cancers.

REFERENCES

Wen, Y., et al. Cancer Sci. 101(11):2325-2332(2010)
Santos, A.M., et al. J. Clin. Invest. 119(12):3613-3625(2009)
Kennedy, A., et al. Int. J. Cancer 124(1):27-35(2009)
Hughes, D.S., et al. BMC Dev. Biol. 9, 30 (2009) :
Cheng, J.D., et al. Mol. Cancer Ther. 4(3):351-360(2005)

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