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Recombinant Mouse Pigment Epithelium-Derived Factor/PEDF/SERPIN F1

Recombinant Mouse Pigment Epithelium-Derived Factor/PEDF/SERPIN F1 Recombinant Mouse Pigment Epithelium-Derived Factor/PEDF/SERPIN F1

Instruction Manual!

Product name: Recombinant Mouse Pigment Epithelium-Derived Factor/PEDF/SERPIN F1
Source:E. coli
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Supplied as a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source E. coli
Description Recombinant Mouse Serpin F1/PEDF is produced by our E.coli expression system and the target gene encoding Asp43-Thr417 is expressed.
Names Pigment epithelium-derived factor, Pedf, Sdf3, Caspin, Serpin F1, Stromal cell-derived factor 3.
Accession # P97298
Formulation Supplied as a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4.
Shipping The product is shipped on dry ice/ice packs.
Storage Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles.
Purity Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence
MDPFFKVPVNKLAAAVSNFGYDLYRLRSSASPTGNVLLSPLSVATALSALSLGAEHRTESVIHRA LYYDLITNPDIHSTYKELLASVTAPEKNLKSASRIVFERKLRVKSSFVAPLEKSYGTRPRILTGN PRVDLQEINNWVQAQMKGKIARSTREMPSALSILLLGVAYFKGQWVTKFDSRKTTLQDFHLDEDR TVRVPMMSDPKAILRYGLDSDLNCKIAQLPLTGSMSIIFFLPLTVTQNLTMIEESLTSEFIHDID RELKTIQAVLTVPKLKLSFEGELTKSLQDMKLQSLFESPDFSKITGKPVKLTQVEHRAAFEWNEE GAGSSPSPGLQPVRLTFPLDYHLNQPFLFVLRDTDTGALLFIGRILDPSST
Background Serpin F1 is secreted Neurotrophic protein and belongs to the serpin family. Serpin F1 Highly expressed in the liver, gastric glandular mucosa and renal tubules. It is also expressed in the brain, heart, lung retina and testes. It induces extensive neuronal differentiation in retinoblastoma cells. It is potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, exhibits no serine protease inhibitory activity.

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