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C538
Recombinant Human Pigment Epithelium-Derived Factor/PEDF
10ug
840
756
现货
国产
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C538
Recombinant Human Pigment Epithelium-Derived Factor/PEDF
50ug
2520
2268
现货
国产
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C538
Recombinant Human Pigment Epithelium-Derived Factor/PEDF
500ug
12320
11088
现货
国产
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C538
Recombinant Human Pigment Epithelium-Derived Factor/PEDF
1mg
17600
15840
现货
国产
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C538
Recombinant Human Serpin F1/PEDF
10ug
840
756
现货
国产
-
C538
Recombinant Human Serpin F1/PEDF
50ug
2520
2268
现货
国产
-
C538
Recombinant Human Serpin F1/PEDF
500ug
12320
11088
现货
国产
-
C538
Recombinant Human Serpin F1/PEDF
1mg
17600
15840
现货
国产
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Catalog# C538 Source HEK293 Description Recombinant Human Serpin F1 produced by transfected human cells is a secreted protein with sequence (Gln20-Pro418) of Human SERPIN F1 fused with a polyhistidine tag at the C-terminus. Names Pigment Epithelium-Derived Factor, PEDF, Cell Proliferation-Inducing Gene 35 Protein, EPC-1, Serpin F1, SERPINF1, PEDF Accession # P36955 Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0 Shipping The product is shipped at ambient temperature. Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in 1X PBS.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.Purity Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. Endotoxin Less than 0.1 ng/μg (1 IEU/μg). Amino Acid Sequence QNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLS VATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLR IKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFK GQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLP LKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFS KITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFI GKILDPRGPVDHHHHHHBackground Serpin F1 is a secreted glycoprotein that belongs to the noninhibitory serpin. It has an alpha/beta core serine-protease inhibitor domain, three major beta-sheets, and ten alpha-helices. As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. They are also involved in activities that extend beyond their ability to inhibit proteases. For instance, they may also regulate blood pressure, angiogenesis, or act as storage/transport proteins. Serpin F1 is a new promising approach for the treatment of osteosarcoma and has been described as a natural angiogenesis inhibitor with neurotrophic and immune-modulation properties. The human serpin superfamily consists of at least 35 members that target not only serine proteases, but also selected cysteine proteases and non-protease proteins. Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.