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DNAJB9 Protein

Dieses Recombinant DNAJB9-Protein wird in Escherichia coli (E. coli) exprimiert.
Produktnummer ABIN7539341

Kurzübersicht für DNAJB9 Protein (ABIN7539341)

Target

Alle DNAJB9 Proteine anzeigen
DNAJB9 (Microvascular Endothelial Differentiation Gene 1 Protein (DNAJB9))

Protein-Typ

Recombinant

Spezies

  • 2
  • 1
Human

Quelle

  • 1
  • 1
  • 1
Escherichia coli (E. coli)

Reinheit

> 95 % by SDS-PAGE
  • Verwendungszweck

    Mdg-1

    Sequenz

    MKHHHHHHSA GLEVLFQGPM ASKSYYDTLG VPKSASERQI KKAFHKLAMK YHPDKNKSPD AEAKFREIAE AYETLSDANR RKEYDTLGHS AFTSGKGQRG SGSSFEQSFN FNFDDLFKDF GFFGQNQNTG SKKRFENHFQ TRQDGGSSRQ RHHFQEFSFG GGLFDDMFED MEKMFSFSGF DSTNQHTVQT ENRFHGSSKH CRTVTQRRGN MVTTYTDCSG Q

    Produktmerkmale

    Length (aa):221
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  • Beschränkungen

    Nur für Forschungszwecke einsetzbar
  • Format

    Lyophilized
  • Target

    DNAJB9 (Microvascular Endothelial Differentiation Gene 1 Protein (DNAJB9))

    Andere Bezeichnung

    Mdg-1

    Hintergrund

    Microvascular endothelial differentiation gene 1 protein, DnaJ homolog subfamily B member 9, ERdj4,Angiogenesis research has focused on receptors and ligands mediating endothelial cell proliferation and migration. Little is known about the molecular mechanisms that are involved in converting endothelial cells from a proliferative to a differentiated state. Microvascular differentiation gene 1 (Mdg1) has been isolated from differentiating microvascular endothelial cells that had been cultured in collagen type I gels (3D culture). In adult human tissue Mdg1 is expressed in endothelial and epithelial cells. Sequence analysis of the full-length cDNA revealed that the N-terminal region of the putative Mdg1-protein exhibits a high sequence similarity to the J-domain of Hsp40 chaperones. It was shown that this region functions as a bona fide J-domain as it can replace the J-domain of Escherichia coli DnaJ-protein. Mdg1 is also upregulated in primary endothelial and mesangial cells when subjected to various stress stimuli. GFP-Mdg1 fusion constructs showed the Mdg1-protein to be localized within the cytoplasm under control conditions. Stress induces the translocation of Mdg1 into the nucleus, where it accumulates in nucleoli. Costaining with Hdj1, Hdj2, Hsp70, and Hsc70 revealed that Mdg1 colocalizes with Hsp70 and Hdj1 in control and stressed HeLa cells. These data suggest that Mdg1 is involved in the control of cell cycle arrest taking place during terminal cell differentiation and under stress conditions.

    Molekulargewicht

    25.3 kDa

    Gen-ID

    4189

    NCBI Accession

    NM_012328, NP_036460

    UniProt

    Q9UBS3

    Pathways

    ER-Nucleus Signaling
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