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Mouse FAP Recombinant Protein (C-FC) (MC440021)

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Overview
Catalog No.MC440021
Description
Recombinant Mouse FAP Protein, C-FC (MC440021) expressed in Mammalian Cells, spanning Leu26-Asp761. Purity: >90% by SDS-PAGE.
Highlights
  • Mammalian Expression — Proper folding and native glycosylation.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemMammalian cells
AccessionP97321
Protein lengthLeu26-Asp761
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesMus musculus (Mouse)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 113.61 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate Names170 kDa melanoma membrane-bound gelatinase, APCE, Antiplasmin-cleaving enzyme FAP, soluble form, Dipeptidyl peptidase FAP, EC:3.4.14.5, EC:3.4.21.-, EC:3.4.21.26, FAP, FAPalpha, Fibroblast activation protein alpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Prolyl endopeptidase FAP, SIMP, Seprase, Serine integral membrane protease, Surface-expressed protease
Background

Prolyl endopeptidase FAP is a ~87 kDa protein. 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. 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).

Note For research use only
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Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
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Formula
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