Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceMQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP

Specifications

Our Abpromise guarantee covers the use of ab56289 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • Endotoxin level< 0.100 Eu/µg
  • Purity> 90 % SDS-PAGE.
    Purity : Greater than 90% by SDS-PAGE gel and HPLC analyses. Endotoxin level is less than 0.1 ng per µg (1EU/µg).
  • FormLyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

General Info

  • Alternative names
    • Cell proliferation-inducing gene 35 protein
    • EPC 1
    • EPC-1
    • EPC1
    • OI12
    • OI6
    • PEDF
    • PEDF_HUMAN
    • PIG 35
    • PIG35
    • Pigment epithelium derived factor
    • Pigment epithelium-derived factor
    • Proliferation inducing protein 35
    • serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1
    • Serpin F1
    • Serpin family F member 1
    • Serpin peptidase inhibitor clade F member 1
    • serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1
    • SERPINF 1
    • Serpinf1
    see all
  • FunctionNeurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor 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.
  • Tissue specificityRetinal pigment epithelial cells and blood plasma.
  • Sequence similaritiesBelongs to the serpin family.
  • Developmental stageExpressed in quiescent cells.
  • DomainThe N-terminal (AA 44-121) exhibits neurite outgrowth-inducing activity. The C-terminal exposed loop (AA 382-418) is essential for serpin activity.
  • Post-translational
    modifications
    The N-terminus is blocked. Extracellular phosphorylation enhances antiangiogenic activity.
    N- and O-glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan.
  • Cellular localizationSecreted. Melanosome. Enriched in stage I melanosomes.
  • Information by UniProt

References for Recombinant Human PEDF protein (ab56289)

This product has been referenced in:
  • Cina DP  et al. Renal tubular angiogenic dysregulation in anti-Thy1.1 glomerulonephritis. Am J Physiol Renal Physiol 300:F488-98 (2011). WB . Read more (PubMed: 21048020) »

See 1 Publication for this product

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"