Name
Recombinant Human PEDF (Recombinant Human Pigment Epithelium-derived Factor; rHuPEDF)；重組人色素上皮衍生因子
Synonyms
EPC-1; PEDF; Cell proliferation-inducing gene 35 protein; EPC-1PIG35; PEDFpigment epithelium-derived factor; pigment epithelium derived factor), member 1; proliferation-inducing protein 35; serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antiplasmin; Serpin F1; serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epitheliumderived factor), member 1
Purity
>97% by SDS-PAGE and HPLC analyses.
Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by its ability to enhance the adhesion of human Saos2 cells to bovine Collagen I coated plate is less than 2ng/ml, corresponding to a specific activity of >5.0×105IU/mg.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM PB, pH7.4, 150mM NaCl.
Endotoxin
Less than 1EU/μg of rHuPEDF as determined by LAL method.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤-20℃. Further dilutions should be made in appropriate buffered solutions.
Background
Pigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418a.a. about 50kDa precursor that contains a 19a.a. signal sequence and a 399a.a. mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity. PEDF has functions of inducing extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. PEDF is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer.
Amino Acid Sequence
QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGP