SCIMP Protein, Human (Cell-Free, His)

SCIMP proteins are lipid tetraspanin-related transmembrane adapters that are critical for orchestrating immune cell signaling. As a scaffold for Src family kinases, it is critical for MHC-II signaling, enhanced calcium responses, and ERK activity in B cells. SCIMP Protein, Human (Cell-Free, His) is the recombinant human-derived SCIMP protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of SCIMP Protein, Human (Cell-Free, His) is 145 a.a., with molecular weight of 22.7 kDa.

SCIMP protein serves as a lipid tetraspanin-associated transmembrane adapter, playing a crucial role in immune cell signaling by acting as a scaffold for Src-family kinases and other signaling proteins. In B cells, SCIMP is essential for major histocompatibility complex class II (MHC-II) signaling transduction, contributing to calcium response and enhancing ERK activity upon MHC-II stimulation. Additionally, in dendritic cells, SCIMP sustains CLEC7A/DECTIN1 signaling after activation by fungal beta-glucans. Acting as an agonist-inducible signaling adapter, SCIMP selectively enables the expression of pro-inflammatory cytokines IL6 and IL12B in macrophages by interacting with Toll-like receptors (TLR1, TLR2, TLR3, TLR4, and TLR7) and serving as a scaffold for phosphorylation by Src-family kinases. SCIMP forms interactions with various proteins, including CD37, CD53, CD81, LYN, CSK, BLNK, GRB2, and TLR4, highlighting its multifaceted role in orchestrating immune cell signaling pathways.

Human

E. coli Cell-free

N-10*His

Q6UWF3 (M1-F145)

388325

MDTFTVQDSTAMSWWRNNFWIILAVAIIVVSVGLGLILYCVCKWQLRRGKKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPLPPRNWPSLEDSSPQEAPSQPPATYSLVNKVKNKKTVSIPSYIEPEDDYDDVEIPANTEKASF

22.7 kDa

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

<1 EU/μg, determined by LAL method.