Artikelnummer: PKSH031775_100μg-ES

Recombinant Human EphB6 Protein (Fc Tag), 100 μg

Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class based on their structures and sequence relationships. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. EphB6 is an unusual Eph receptor; lacking catalytic capacity due to alterations in its kinase domain. Interestingly; increased metastatic activity is associated with reduced EphB6 receptor expression in several tumor types; including breast cancer. This emphasizes the potential of EphB6 to act as a suppressor of cancer aggressiveness. EphB6 suppress cancer invasiveness through c-Cbl-dependent signaling; morphologic changes; and cell attachment and indicate that EphB6 may represent a useful prognostic marker and a promising target for therapeutic approaches. EphB6 can both positively and negatively regulate cell adhesion and migration; and suggest that tyrosine phosphorylation of the receptor by an Src family kinase acts as the molecular switch for the functional transition. In addition; Ephrin-B2 may be a physiological ligand for the EphB6 receptor.

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Grundlegende Informationen

Marken: Elabscience

Versand: This product is provided as lyophilized powder which is shipped with ice packs.

Speicher: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

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Herkunftsort: China

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Calculated Molecular Weight:86.5 kDa

Observed Molecular Weight:100-110 kDa

Purity: > 90 % as determined by reducing SDS-PAGE.

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Storage:Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

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Calculated Molecular Weight:86.5 kDa

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Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

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Reinheit: > 90 % as determined by reducing SDS-PAGE.

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