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Human B-cell Linker Protein, BLNK ELISA Kit , 96T Mammalian Expression Metallocarboxypeptidase that mediates deglutamylation of
Human B-cell Linker Protein, BLNK ELISA Kit , 96T Mammalian Expression Metallocarboxypeptidase that mediates deglutamylation of
Human B-cell Linker Protein, BLNK ELISA Kit , 96T Mammalian Expression Metallocarboxypeptidase that mediates deglutamylation of
Human B-cell Linker Protein, BLNK ELISA Kit , 96T Mammalian Expression Metallocarboxypeptidase that mediates deglutamylation of

Human B-cell Linker Protein, BLNK ELISA Kit , 96T Mammalian Expression Metallocarboxypeptidase that mediates deglutamylation of

SKU: 11891734195

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Human B-cell Linker Protein, BLNK ELISA Kit , 96T Mammalian Expression Metallocarboxypeptidase that mediates deglutamylation ofFunctions as a central linker protein, downstream of the B cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B cell function and development. Plays a role in the activation of ERK EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF kappa B and NFAT. Plays an important role in BCR mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and

Store: matisco.be · Domain: matisco.be

Description

Metallocarboxypeptidase that mediates deglutamylation of target proteins

the biological significance of the two forms is not known

is generated in pathophysiologic conditions such as inflammation

This protein can promote proteolysis of Yy1

Human B-cell Linker Protein, BLNK ELISA Kit , 96T Mammalian Expression Metallocarboxypeptidase that mediates deglutamylation ofFunctions as a central linker protein, downstream of the B cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B cell function and development. Plays a role in the activation of ERK EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF kappa B and NFAT. Plays an important role in BCR mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and

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