Recombinant Human Serpin F1/PEDF Protein

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SDS-Page: Human Serpin F1/PEDF Protein [NBP2-35205]

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Func, PAGE, Bioactivity
Format
Carrier-Free
Concentration
LYOPH

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Recombinant Human Serpin F1/PEDF Protein Summary

Description
A single, non-glycosylated biologically active polypeptide chain corresponding to 399 residues of SERPINF1.

Source: E. coli

Amino Acid Sequence: QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVLLSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSASRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEIPDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDLSCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKLSYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQPAHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGP

Preparation
Method
Novus' biologically active proteins are stringently purified to provide only the safest and most highly effective proteins available. This protein was expressed in E. coli, purified by HPLC, QC tested by SDS-PAGE and Western Blot and validated on appropriate cell lines for bioactivity. All HPLC and bioactivity data is provided for your assurance.
Details of Functionality
PEDF Protein is 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 x 10^5 IU/mg.
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
SERPINF1
Purity
> 97 % pure by SDS-PAGE and HPLC
Endotoxin Note
Less than 1 EU/ug of endotoxin as determined by LAL method.

Applications/Dilutions

Theoretical MW
44.4 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at -20C. Avoid freeze-thaw cycles.
Buffer
Lyophilized from a 0.2 um filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl.
Concentration
LYOPH
Purity
> 97 % pure by SDS-PAGE and HPLC
Reconstitution Instructions
Reconstitute with sterilized distilled water or 0.1% BSA aqueous buffer to a final concentration of 0.1 - 1.0 mg/ml.

Notes

This lyophilized preparation is stable at 2-8 degrees C, but should be kept at -20 degrees C for long term storage, preferably desiccated. Upon reconstitution, the preparation is most stable at -20 to -80 degrees C, and can be stored for one week at 2-8 degrees C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 degrees C to -80 degrees C. Avoid repeated freeze/thaw cycles.

Alternate Names for Recombinant Human Serpin F1/PEDF Protein

  • Cell 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 antiplasmin
  • Serpin F1
  • serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epitheliumderived factor), member 1

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 418 a.a. about 50 kDa 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 beta-sheets, 810 alpha-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

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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Bioinformatics

Gene Symbol SERPINF1
Entrez
Uniprot