Overview

Description

  • Nature

    Recombinant
  • Source

    EBNA 293 cells
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Amino acids

      20 to 478

Specifications

Our Abpromise guarantee covers the use of ab54116 in the following tested applications.

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

  • Applications

    Functional Studies

    Western blot

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 7.50
    Constituents: 0.242% Tris, 1.16% Sodium chloride

General Info

  • Alternative names

    • Complement S Protein
    • Epibolin
    • S Protein
    • S-protein
    • Serum Spreading Factor
    • Serum-spreading factor
    • Somatomedin B
    • Somatomedin-B
    • V75
    • Vitronectin
    • 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

This product has been referenced in:

  • Lutz R  et al. Pericellular fibronectin is required for RhoA-dependent responses to cyclic strain in fibroblasts. J Cell Sci 123:1511-21 (2010). Functional Studies . Read more (PubMed: 20375066) »
See 1 Publication for this product

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