CBLC Protein, Human (sf9)

CBLC protein is an E3 ubiquitin-protein ligase that plays a crucial regulatory role in the ubiquitin-proteasome system by accepting ubiquitin from specific E2 enzymes and promoting substrate degradation. It forms a functional complex with UB2D1, UB2D2 and UB2D3. CBLC Protein, Human (sf9) is the recombinant human-derived CBLC, expressed by Sf9 insect cells , with tag Free labeled tag. The total length of CBLC Protein, Human (sf9) is 473 a.a.,

CBLC protein functions as an E3 ubiquitin-protein ligase, playing a crucial role in the ubiquitin-proteasome system by accepting ubiquitin from specific E2 ubiquitin-conjugating enzymes and transferring it to substrates, thereby promoting their degradation. It forms a functional complex with E2 ubiquitin-protein ligases UB2D1, UB2D2, and UB2D3. CBLC acts as a regulator in EGFR-mediated signal transduction, where upon EGF activation, it ubiquitinates EGFR, leading to its degradation. Isoform 1, in contrast to isoform 2, inhibits MAPK1 activation stimulated by EGF. Additionally, CBLC promotes the ubiquitination of SRC phosphorylated at 'Tyr-419'. In collaboration with CD2AP, CBLC serves as a regulatory checkpoint for Ret signaling by modulating the rate of RET degradation following ligand activation. The partnership with CD2AP transforms CBLC from an inhibitor to a promoter of RET degradation, limiting the potency of GDNF on neuronal survival in the process.

Human

Sf9 insect cells

Tag Free

Q9ULV8-1 (A2-A474)

23624

52.4 KDa

Greater than 90 % as determined by reducing SDS-PAGE.

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