Native Rat Vitronectin/S-Protein (ab92745)
Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
Description
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Product name
Native Rat Vitronectin/S-Protein
See all Vitronectin/S-Protein proteins and peptides -
Purity
> 95 % SDS-PAGE. -
Expression system
Native -
Protein length
Full length protein -
Animal free
No -
Nature
Native -
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Species
Rat
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab92745 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Liquid -
Additional notes
Spectrophotometric Data: Ultraviolet: Absorbance (280nm) = 3.23 epsilon 0.1% = 1.38 -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.40
Constituents: 0.82% Sodium phosphate, 0.58% Sodium chloride
General Info
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Alternative names
- Complement S Protein
- Epibolin
- S Protein
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
modificationsSulfated 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
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab92745 has not yet been referenced specifically in any publications.