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Recombinant Human Serpin F1/PEDF Protein, >97%(SDS-PAGE, HPLC), high purity

  • ActiBioPure™
  • Animal Free
  • Azide Free
  • Bioactive
  • Carrier Free
  • High performance
  • ≥97%(SDS-PAGE&HPLC)
Features and benefits
  • Expression System: E.coli
  • Accession #: P36955
  • Protein Tag: No tag
  • Bioactivity: 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 2 ng/ml.
  • Endotoxin Concentration: <1 EU/μg
Item Number
rp150051
Grouped product items
SKUSizeAvailabilityPrice Qty
rp150051-10μg
10μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$69.90
rp150051-50μg
50μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$329.90
rp150051-100μg
100μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$399.90
rp150051-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$4,999.90

Animal Free, >97%(SDS-PAGE, HPLC), Active, E.coli, No tag, 20-418 aa

Basic Description

Product NameRecombinant Human Serpin F1/PEDF Protein, >97%(SDS-PAGE, HPLC), high purity
SynonymsCell proliferation-inducing gene 35 protein; EPC-1; EPC-1PIG35; PEDF; PEDFpigment epithelium-derived factor; pigment epithelium derived factor), member 1; proliferation-inducing protein 35; serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antip
GradeActiBioPure™, Animal Free, Azide Free, Bioactive, Carrier Free, High performance
Product Description

Purity

>97% by SDS-PAGE and HPLC analyses.


Function

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 418 a.a. about 50kDa precursor that contains a 19 a.a. signal sequence and a 399 a.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.


Specifications & PurityActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, High performance, ≥97%(SDS-PAGE&HPLC)
Purity>97%(SDS-PAGE, HPLC)
BioactivityFully 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 2 ng/ml.
Endotoxin Concentration<1 EU/μg
Expression SystemE.coli
SpeciesHuman
Amino Acids20-418 aa
SequenceQNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VL
Protein TagNo tag
Accession #P36955
Predicted molecular weight44.4kDa

Images

Recombinant Human Serpin F1/PEDF (rp150051)-Protein Bioactivity
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 2 ng/mL, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

Recombinant Human Serpin F1/PEDF (rp150051) -SDS-PAGE
Recombinant Human Serpin F1/PEDF Protein was resolved with SDS-PAGE under reducing (R) and visualized by Coomassie® Blue staining, showing a single band at 44.4 kDa.

Product Specifications

FormLyophilized
ReconstitutionWe 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 0.1-1.0 mg/mL. Stock solutions should be apportio
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InDry ice
Stability And StorageUse a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 ℃ as supplied. 1 month, 2 to 8 ℃ under sterile conditions after reconstitution. 3 months, -20 to -70 ℃ under sterile conditions after reconstitu

Certificates

Certificate of Analysis(COA)

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3 results found

Lot NumberCertificate TypeDateItem
ZJ23F0600476Certificate of AnalysisMar 26, 2024 rp150051
ZJ23F0600477Certificate of AnalysisMar 26, 2024 rp150051
ZJ23F0600478Certificate of AnalysisMar 26, 2024 rp150051

Related Documents

References

1. Tan L, Gurbani D, Weisberg EL, Jones DS, Rao S, Singer WD, Bernard FM, Mowafy S, Jenney A, Du G et al..  (2017)  Studies of TAK1-centered polypharmacology with novel covalent TAK1 inhibitors..  Bioorg Med Chem,  25  (4): (1320-1328).  [PMID:28038940]
2. Thomas R Burkard,Melanie Planyavsky,Ines Kaupe,Florian P Breitwieser,Tilmann Bürckstümmer,Keiryn L Bennett,Giulio Superti-Furga,Jacques Colinge.  (2011-01-29)  Initial characterization of the human central proteome..  BMC systems biology,  (17-17).  [PMID:21269460]
3. Becerra, S P SP, Sagasti, A A, Spinella, P P and Notario, V V..  (1995)  Pigment epithelium-derived factor behaves like a noninhibitory serpin. Neurotrophic activity does not require the serpin reactive loop..  The Journal of biological chemistry,    (27):   [PMID:7592790]
4. Becerra, S P SP and 6 more authors..  (1993)  Overexpression of fetal human pigment epithelium-derived factor in Escherichia coli. A functionally active neurotrophic factor..  The Journal of biological chemistry,    (5):   [PMID:8226833]
5. Steele, F R FR, Chader, G J GJ, Johnson, L V LV and Tombran-Tink, J J..  (1993)  Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family..  Proceedings of the National Academy of Sciences of the United States of America,    (15):   [PMID:8434014]
6. Pignolo, R J RJ, Cristofalo, V J VJ and Rotenberg, M O MO..  (1993)  Senescent WI-38 cells fail to express EPC-1, a gene induced in young cells upon entry into the G0 state..  The Journal of biological chemistry,    (25):   [PMID:8473338]
7. Tombran-Tink, J J and 6 more authors..  (1996)  Organization, evolutionary conservation, expression and unusual Alu density of the human gene for pigment epithelium-derived factor, a unique neurotrophic serpin..  Molecular vision,    (4):   [PMID:9238088]
8. Koenekoop, R R and 6 more authors..  (1999)  Four polymorphic variations in the PEDF gene identified during the mutation screening of patients with Leber congenital amaurosis..  Molecular vision,    (2):   [PMID:10398730]
9. Simonovic, M M, Gettins, P G PG and Volz, K K..  (2001)  Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor..  Proceedings of the National Academy of Sciences of the United States of America,    (25):   [PMID:11562499]
10. Petersen, Steen V SV, Valnickova, Zuzana Z and Enghild, Jan J JJ..  (2003)  Pigment-epithelium-derived factor (PEDF) occurs at a physiologically relevant concentration in human blood: purification and characterization..  The Biochemical journal,    (15):   [PMID:12737624]
11. Maik-Rachline, Galia G, Shaltiel, Shmuel S and Seger, Rony R..  (2005)  Extracellular phosphorylation converts pigment epithelium-derived factor from a neurotrophic to an antiangiogenic factor..  Blood,    (15):   [PMID:15374885]
12. Liu, Tao T and 6 more authors..  ()  Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry..  Journal of proteome research,      [PMID:16335952]
13. Zody, Michael C MC and 73 more authors..  (2006)  DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage..  Nature,    (20):   [PMID:16625196]
14. Notari, Luigi L and 12 more authors..  (2006)  Identification of a lipase-linked cell membrane receptor for pigment epithelium-derived factor..  The Journal of biological chemistry,    (8):   [PMID:17032652]
15. Chi, An A and 16 more authors..  (2006)  Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes..  Journal of proteome research,      [PMID:17081065]
16. Becker, Jutta J and 16 more authors..  (2011)  Exome sequencing identifies truncating mutations in human SERPINF1 in autosomal-recessive osteogenesis imperfecta..  American journal of human genetics,    (11):   [PMID:21353196]
17. Oshikawa, Mio M and 8 more authors..  (2011)  Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method..  Investigative ophthalmology & visual science,    (22):   [PMID:21697133]
18. Rosenow, Anja A and 6 more authors..  (2012)  Resveratrol-induced changes of the human adipocyte secretion profile..  Journal of proteome research,    (7):   [PMID:22905912]

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