Description

  • Product name

    Recombinant human Protein C
    See all Protein C proteins and peptides
  • Biological activity

    Specific Activity: 90 pmol/min/µg.

    Assay Conditions: 50 mM Tris-HCl, pH 8.5, 150 mM NaCl, 10 mM CaCl2, 0.01% Brij-35, 100 µM substrate, and various amounts of Activated Protein C. Incubate for 10 minutes at room temperature. Fluorescence intensity is measured at exc380/em460.

  • Purity

    > 90 % SDS-PAGE.

  • Expression system

    HEK 293 cells
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MWQLTSLLLF VATWGISGTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL RHSSLERECI EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP CASLCCGHGT CIDGIGSFSC DCRSGWEGRF CQREVSFLNC SLDNGGCTHY CLEEVGWRRC SCAPGYKLGD DLLQCHPAVK FPCGRPWKRM EKKRSHLKRD TEDQEDQVDP RLIDGKMTRR GDSPWQVVLL DSKKKLACGA VLIHPSWVLT AAHCMDESKK LLVRLGEYDL RRWEKWELDL DIKEVFVHPN YSKSTTDNDI ALLHLAQPAT LSQTIVPICL PDSGLAEREL NQAGQETLVT GWGYHSSREK EAKRNRTFVL NFIKIPVVPH NECSEVMSNM VSENMLCAGI LGDRQDACEG DSGGPMVASF HGTWFLVGLV SWGEGCGLLH NYGVYTKVSR YLDWIHGHIR DKEAPQKSWA P
    • Predicted molecular weight

      52 kDa
    • Amino acids

      1 to 461
    • Tags

      His tag C-Terminus
    • Additional sequence information

      NM_000312.

Specifications

Our Abpromise guarantee covers the use of ab198147 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

    Functional Studies

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.

    pH: 8.50
    Preservative: 1.7% Imidazole
    Constituents: 0.79% Tris HCl, 0.8% Sodium chloride, 0.02% Potassium chloride

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names

    • Activation peptide
    • Anticoagulant protein C
    • APC
    • Autoprothrombin IIA
    • Blood coagulation factor XIV
    • EC 3.4.21.69
    • PC
    • proC
    • PROC_HUMAN
    • PROC1
    • Protein C (inactivator of coagulation factors Va and VIIIa)
    • THPH3
    • THPH4
    • Vitamin K dependent protein C
    see all
  • Function

    Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts a protective effect on the endothelial cell barrier function (PubMed:25651845).
  • Tissue specificity

    Plasma; synthesized in the liver.
  • Involvement in disease

    Thrombophilia due to protein C deficiency, autosomal dominant
    Thrombophilia due to protein C deficiency, autosomal recessive
  • Sequence similarities

    Belongs to the peptidase S1 family.
    Contains 2 EGF-like domains.
    Contains 1 Gla (gamma-carboxy-glutamate) domain.
    Contains 1 peptidase S1 domain.
  • Post-translational
    modifications

    The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.
    N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not N-glycosylated at Asn-371, is beta. O-glycosylated with core 1 or possibly core 8 glycans.
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
    May be phosphorylated on a Ser or Thr in a region (AA 25-30) of the propeptide.
  • Cellular localization

    Secreted. Golgi apparatus. Endoplasmic reticulum.
  • Information by UniProt

Images

  • Specific activity of ab198147.

  • 4-20% SDS-PAGE analysis of ab198147 (3 µg) with Coomassie staining.

    Note: Protein is secreted and converted to the active form with disulfide link (light chain a.a. 43-199, heavy chain a.a. 212-461). The signal peptide (a.a. 1-32), propeptide (a.a. 33-42), and activation peptide (a.a. 200-211) are cleaved. MW = ~60 kDa, ~42 kDa, ~20 kDa under reducing conditions.

References

ab198147 has not yet been referenced specifically in any publications.

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