Recombinant Mouse Periostin protein (His tag)
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(1 Publication)
Recombinant Mouse Periostin protein (His tag) is a Mouse Full Length protein, in the 1 to 811 aa range, expressed in HEK 293 cells, with >92%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
Osf2, Postn, Periostin, PN, Osteoblast-specific factor 2, OSF-2
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Mouse Periostin protein (His tag) (AB276845)
SDS-PAGE analysis of ab276845
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The periostin protein contributes to the maintenance of tissue integrity and mechanical properties. It does not solely act; it forms part of a multiprotein complex with collagen and other extracellular matrix components. This involvement is necessary for maintaining cellular interactions and promoting tissue healing processes. Additionally periostin influences cell proliferation and migration impacting developmental and wound healing biology.
Pathways
Periostin is involved in the integrin signaling pathway and the Wnt/β-catenin pathway both important for cell communication and movement. Through these pathways periostin interacts with integrins αvβ3 and αvβ5 facilitating cell adhesion and migration. The Wnt/β-catenin pathway interaction involves several proteins including Frizzled receptors ensuring regulation of cellular proliferation and differentiation. These pathways make periostin a coordinator of complex cellular processes.
Specifications
Form
Lyophilized
General info
Function
Induces cell attachment and spreading and plays a role in cell adhesion (PubMed : 10404027). Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (PubMed : 20181949).
Post-translational modifications
Gamma-carboxylation is controversial. Gamma-carboxyglutamated; gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation; these residues may be required for binding to calcium (PubMed:18450759). According to a more recent report in human, does not contain vitamin K-dependent gamma-carboxyglutamate residues (By similarity).
Target data
Publications (1)
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Pharmacology 108:432-443 PubMed37343534
2023
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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