protein

CBLB/RNF56 Protein, Human (HEK293, His)

HY-P78728

5 μg;10 μg;50 μg

50;80;220 USD

CBLB/RNF56 Protein, Human (HEK293, His)

proteins

HEK293

5 μg;10 μg;50 μg

50;80;220 USD

The CBLB/RNF56 protein is an E3 ubiquitin protein ligase that coordinates substrate degradation through ubiquitin transfer by specific E2 enzymes. It crucially inhibits signal transduction pathways initiated by TCR, BCR and FCER1. CBLB/RNF56 Protein, Human (HEK293, His) is the recombinant human-derived CBLB/RNF56 protein, expressed by HEK293 , with N-His labeled tag. The total length of CBLB/RNF56 Protein, Human (HEK293, His) is 388 a.a.

Human

CBLB/RNF56 Protein serves as an E3 ubiquitin-protein ligase, mediating the transfer of ubiquitin from specific E2 ubiquitin-conjugating enzymes to substrates, ultimately promoting their degradation by the proteasome. It plays a pivotal role in negatively regulating signal transduction pathways initiated by TCR, BCR, and FCER1. In naive T-cells, CBLB inhibits VAV1 activation upon TCR engagement and mandates CD28 costimulation for proliferation and IL-2 production. Furthermore, it promotes ubiquitination of PIK3R1/p85, hindering its recruitment to the TCR and subsequent activation. In activated T-cells, CBLB hampers PLCG1 activation and calcium mobilization upon restimulation, contributing to the induction of anergy. In B-cells, it ubiquitinates SYK, facilitating its proteasomal degradation. Additionally, CBLB may play a role in SRC ubiquitination and could be involved in EGFR ubiquitination and internalization. It is suggested to work in conjunction with the E2 ubiquitin-protein ligase UB2D3 and, when associated with CBL, is essential for the proper feedback inhibition of ciliary PDGFRA signaling through ubiquitination and internalization of PDGFRA.

CBL-B; CBLB; RNF56

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized a 0.22 μm filtered solution of 40 mM HEPES, 120 mM NaCl, pH 6.8, 8% trehalose.

Room temperature in continental US; may vary elsewhere.