Natural Human Vitronectin protein (ab82274)

Overview

Description

  • Nature
    Native
  • Source
    Native
  • Amino Acid Sequence
    • Species
      Human

Specifications

Our Abpromise guarantee covers the use of ab82274 in the following tested applications.

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

  • Biological activity
    Second order rate constants for inhibition of: uPA = 6.3 x 106 M-1s-1 tPA = 5.7 x 106 M-1s-1
  • Applications

    SDS-PAGE

  • Purity
    > 95 % SDS-PAGE.
    >98% pure (SDS-PAGE). Column chromatography
  • Form
    Liquid
  • Additional notes
    Second order rate constants for inhibition of: uPA = 6.3 x 106 M-1s-1 tPA = 5.7 x 106 M-1s-1
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 50mM Sodium phosphate, 100mM Sodium chloride, pH 7.4

General Info

  • Alternative names
    • Complement S Protein
    • Epibolin
    • S Protein
    • S-protein
    • Serum Spreading Factor
    • Serum-spreading factor
    • Somatomedin B
    • Somatomedin-B
    • V75
    • Vitronectin V10 subunit
    • Vitronectin V65 subunit
    • VN
    • VNT
    • VTN
    • VTNC_HUMAN
    see all
  • Function
    Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.
    Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
  • Tissue specificity
    Plasma.
  • Sequence similarities
    Contains 4 hemopexin repeats.
    Contains 1 SMB (somatomedin-B) domain.
  • Domain
    The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.
  • Post-translational
    modifications
    Sulfated on 2 tyrosine residues.
    N- and O-glycosylated.
    Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading.
    It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.
    Phosphorylation sites are present in the extracellular medium.
  • Cellular localization
    Secreted, extracellular space.
  • Information by UniProt

References

ab82274 has not yet been referenced specifically in any publications.

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

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