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FAP Protein (AA 24-761) (rho-1D4 tag)

Crystallography grade FAP Origine: Souris Hôte: Cellules d'insectes Recombinant >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. WB, SDS, ELISA, Crys
N° du produit ABIN3134684
  • Antigène Voir toutes FAP Protéines
    FAP (Fibroblast Activation Protein, alpha (FAP))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 24-761
    Origine
    • 18
    • 9
    • 3
    • 3
    Souris
    Source
    • 18
    • 6
    • 3
    • 2
    • 2
    • 1
    Cellules d'insectes
    Purification/Conjugué
    Cette FAP protéine est marqué à la rho-1D4 tag.
    Application
    Western Blotting (WB), SDS-PAGE (SDS), ELISA, Crystallization (Crys)
    Séquence
    IVLRPSRVYK PEGNTKRALT LKDILNGTFS YKTYFPNWIS EQEYLHQSED DNIVFYNIET RESYIILSNS TMKSVNATDY GLSPDRQFVY LESDYSKLWR YSYTATYYIY DLQNGEFVRG YELPRPIQYL CWSPVGSKLA YVYQNNIYLK QRPGDPPFQI TYTGRENRIF NGIPDWVYEE EMLATKYALW WSPDGKFLAY VEFNDSDIPI IAYSYYGDGQ YPRTINIPYP KAGAKNPVVR VFIVDTTYPH HVGPMEVPVP EMIASSDYYF SWLTWVSSER VCLQWLKRVQ NVSVLSICDF REDWHAWECP KNQEHVEESR TGWAGGFFVS TPAFSQDATS YYKIFSDKDG YKHIHYIKDT VENAIQITSG KWEAIYIFRV TQDSLFYSSN EFEGYPGRRN IYRISIGNSP PSKKCVTCHL RKERCQYYTA SFSYKAKYYA LVCYGPGLPI STLHDGRTDQ EIQVLEENKE LENSLRNIQL PKVEIKKLKD GGLTFWYKMI LPPQFDRSKK YPLLIQVYGG PCSQSVKSVF AVNWITYLAS KEGIVIALVD GRGTAFQGDK FLHAVYRKLG VYEVEDQLTA VRKFIEMGFI DEERIAIWGW SYGGYVSSLA LASGTGLFKC GIAVAPVSSW EYYASIYSER FMGLPTKDDN LEHYKNSTVM ARAEYFRNVD YLLIHGTADD NVHFQNSAQI AKALVNAQVD FQAMWYSDQN HGISSGRSQN HLYTHMTHFL KQCFSLSD
    Sequence without tag. Tag location is at the discretion of the manufacturer. If you have a special request, please contact us.
    Attributs du produit
    • Made in Germany - from design to production - by highly experienced protein experts.
    • Mouse Fap Protein (raised in Insect Cells) purified by multi-step, protein-specific process to ensure crystallization grade.
    • State-of-the-art algorithm used for plasmid design (Gene synthesis).

    This protein is a made to order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

    The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

    In the unlikely event that the protein cannot be expressed or purified we do not charge anything (other companies might charge you for any performed steps in the expression process for custom-made proteins, e.g. fees might apply for the expression plasmid, the first expression experiments or purification optimization).

    When you order this made-to-order protein you will only pay upon receival of the correctly folded protein. With no financial risk on your end you can rest assured that our experienced protein experts will do everything to make sure that you receive the protein you ordered.

    The concentration of our recombinant proteins is measured using the absorbance at 280nm. The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.

    The concentration of the protein is calculated using its specific absorption coefficient. We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

    Purification
    Three step purification of membrane proteins expressed in baculovirus infected SF9 insect cells:
    1. Membrane proteins are fractioned by ultracentrifugation and subsequently solubilized with different detergents (detergent screen). Samples are analyzed by Western blot.
    2. The best performing detergent is used for solubilization and the proteins are purified via their rho1D4 tag via two rho1D4 antibody columns: one DTT resistant, the other one not. Eluate fractions are analyzed by Western blot.
    3. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatograph. Eluate fractions are analyzed by SDS-PAGE and Western blot.
    Pureté
    >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
    Stérilité
    0.22 μm filtered
    niveau d'endotoxine
    Protein is endotoxin-free.
    Classe de qualité
    Crystallography grade
    Top Product
    Discover our top product FAP Protéine
  • Indications d'application
    In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a gurantee though.
    Commentaires

    Protein has not been tested for activity yet. In cases in which it is highly likely that the recombinant protein with the default tag will be insoluble our protein lab may suggest a higher molecular weight tag (e.g. GST-tag) instead to increase solubility. We will discuss all possible options with you in detail to assure that you receive your protein of interest.

    Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    100 mM NaCL, 20 mM Hepes, 10% glycerol. pH value is at the discretion of the manufacturer.
    Conseil sur la manipulation
    Avoid repeated freeze-thaw cycles.
    Stock
    -80 °C
    Stockage commentaire
    Store at -80°C.
    Date de péremption
    Unlimited (if stored properly)
  • Antigène
    FAP (Fibroblast Activation Protein, alpha (FAP))
    Autre désignation
    Fap (FAP Produits)
    Synonymes
    fap-A Protein, gene 13 Protein, FAP Protein, fapa Protein, dppiv Protein, seprase Protein, DPPIV Protein, FAPA Protein, fibroblast activation protein Protein, fibroblast activation protein alpha L homeolog Protein, fibroblast activation protein alpha Protein, fibroblast activation protein, alpha Protein, prolyl endopeptidase FAP Protein, Fap Protein, fap.L Protein, FAP Protein, fap Protein, LOC100547273 Protein
    Sujet
    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. {ECO:0000269|PubMed:10629066, ECO:0000269|PubMed:11330865, ECO:0000269|PubMed:15133496, ECO:0000269|PubMed:21051638, ECO:0000269|PubMed:23710635, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:9688278}.
    Poids moléculaire
    86.7 kDa Including tag.
    UniProt
    P97321
    Pathways
    Tube Formation
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