Human Serpin F1 / PEDF Protein, His Tag

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SE1-H5221-100ug
$315.00
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SE1-H5221-1mg (250ug X 4)
$1,950.00
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SE1-H5221
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Synonyms

SERPINF1, Serpin F1, PEDF, PIG35, EPC-1

Source

Human Serpin F1, His Tag (SE1-H5221) is expressed from human 293 cells (HEK293). It contains AA Gln 20 - Pro 418 (Accession # NP_002606).

Predicted N-terminus: Gln 20

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 45.2 kDa. The protein migrates as 45-60 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>90% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

Introduction de fond

erpin F1 (SERPINF1) is also known as Pigment epithelium-derived factor (PEDF), Cell proliferation-inducing gene 35 protein (PIG35). Serpin F1 belongs to the serpin family. Serpin F1 is expressed in quiescent cells. PEDF has a variety of functions including antiangiogenic, antitumorigenic, and neurotrophic properties. Endothelial cell migration is inhibited by SERPINF1/ PEDF. PEDF / SERPINF1 suppresses retinal neovascularization and endothelial cell proliferation. PEDF is also responsible for apoptosis of endothelial cells either through the p38 MAPK pathway or through the FAS/FASL pathway. PEDF also displays neurotrophic functions.