Thermo Fisher Scientific Human Osteopontin Recombinant Protein, PeproTech

Applications

Tested Dilution

Publications

Western Blot (WB)

Assay-dependent

-

ELISA (ELISA)

Assay-dependent

-

Functional Assay (Functional)

Assay-dependent

-

In vitro Assay (IV)

-

View 8 publications 8 publications

Miscellaneous PubMed (Misc)

-

View 1 publication 1 publication

Product Specifications

Species

Human

Published species

Human, Mouse

Expression System

HEK293 cells

Amino acid sequence

IPVKQADSGS SEEKQLYNKY PDAVATWLNP DPSQKQNLLA PQNAVSSEET NDFKQETLPS KSNESHDHMD DMDDEDDDDH VDSQDSIDSN DSDDVDDTDD SHQSDESHHS DESDELVTDF PTDLPATEVF TPVVPTVDTY DGRGDSVVYG LRSKSKKFRR PDIQYPDATD EDITSHMESE ELNGAYKAIP VAQDLNAPSD WDSRGKDSYE TSQLDDQSAE THSHKQSRLY KRKANDESNE HSDVIDSQEL SKVSREFHSH EFHSHEDMLV VDPKSKEEDK HLKFRISHEL DSASSEVN

Molecular weight

33.7 kDa

Class

Recombinant

Type

Protein

Purity

≥ 97% by SDS-PAGE gel and HPLC analyses.

Endotoxin concentration

<1 EU/µg

Activity

Determined by its ability to enhance cell adhesion of murine B16-F1 cells.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient

Product Specific Information

Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE analysis under reducing conditions.

This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Target Information

Osteopontin is an arginine-glycine-aspartic acid (RGD)-containing glycoprotein that interacts with integrins and CD44 as major receptors. It is a multifunctional protein involved in bone mineralization, cell adhesion, cell migration, chronic inflammatory disease and transformation. Proteolytic cleavage by thrombin and matrix metalloproteinases close to the integrin-binding Arg-Gly-Asp sequence modulates the function of OPN and its integrin binding properties. Thrombin-cleaved fragments of Osteopontin are overexpressed in malignant glial tumors and provide a molecular niche with survival advantage and provide a novel substrate for plasmin and cathepsin D.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.