SLURP2 Protein, Human (P.pastoris, His)

SLURP2 protein affects keratinocyte proliferation, differentiation, and apoptosis by binding to and potentially modulating nicotinic and muscarinic acetylcholine receptors. In vitro studies have shown that SLURP2 has a moderate inhibitory effect on nAChRs containing α-3:β-2, a strong inhibitory effect on nAChRs containing α-4:β-2, regulates nAChRs containing α-7, and inhibits Nicotine-induced signaling may involve nAChRs containing α-3:β-4. SLURP2 Protein, Human (P.pastoris, His) is the recombinant human-derived SLURP2 protein, expressed by P. pastoris , with N-His labeled tag. The total length of SLURP2 Protein, Human (P.pastoris, His) is 75 a.a., with molecular weight of ~10.0 kDa.

The SLURP2 protein plays a regulatory role by binding to and potentially modulating the functional properties of both nicotinic and muscarinic acetylcholine receptors. Its involvement extends to the regulation of keratinocyte proliferation, differentiation, and apoptosis. In vitro studies reveal that SLURP2 moderately inhibits acetylcholine-evoked currents of alpha-3:beta-2-containing nAChRs, strongly inhibits those of alpha-4:beta-2-containing nAChRs, modulates alpha-7-containing nAChRs, and inhibits nicotine-induced signaling, likely implicating alpha-3:beta-4-containing nAChRs. The protein is proposed to act on alpha-3:beta-2 and alpha-7 nAChRs in an orthosteric manner and on mAChRs, such as CHRM1 and CHRM3, in an allosteric manner. Interactions with specific subunits (CHRNA3, CHRNA4, CHRNA5, CHRNA7, CHRNB2, and CHRNB4) and with CHRM1 and CHRM3, likely in an allosteric manner, have been observed.

Human

P. pastoris

N-His

P0DP57 (23I-97D)

432355  [NCBI]

IWCHQCTGFGGCSHGSRCLRDSTHCVTTATRVLSNTEDLPLVTKMCHIGCPDIPSLGLGPYVSIACCQTSLCNHD

Approximately 10.0 kDa

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

<1 EU/μg, determined by LAL method.