protein

STIM1 Protein, Human (HEK293, His)

HY-P74536

5 μg;10 μg;50 μg;100 μg;500 μg

35;40;105;180;620 USD

STIM1 Protein, Human (HEK293, His)

proteins

HEK293

5 μg;10 μg;50 μg;100 μg;500 μg

35;40;105;180;620 USD

STIM1 (stromal interacting molecule 1) coordinates store-operated Ca(2+) entry (SOCE) and acts as a Ca(2+) sensor in the endoplasmic reticulum. Upon Ca(2+) depletion, STIM1 translocates to the plasma membrane and activates the Ca(2+)-releasing activated Ca(2+) (CRAC) channel subunit ORAI1. STIM1 Protein, Human (HEK293, His) is the recombinant human-derived STIM1 protein, expressed by HEK293 , with C-His labeled tag. The total length of STIM1 Protein, Human (HEK293, His) is 191 a.a., with molecular weight of 27-34 kDa.

Human

STIM1 (Stromal interaction molecule 1) plays a pivotal role in mediating store-operated Ca(2+) entry (SOCE), a process that involves Ca(2+) influx following the depletion of intracellular Ca(2+) stores. Functioning as a Ca(2+) sensor in the endoplasmic reticulum through its EF-hand domain, STIM1 translocates from the endoplasmic reticulum to the plasma membrane upon Ca(2+) depletion. In this activated state, it interacts with and activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1. STIM1 forms homooligomers and heterooligomers with STIM2, and its interaction with other proteins, such as SPPL3, MAPRE1, CRACR2A/EFCAB4B, SARAF, EFHB, ASPH, SLC35G1, TMEM203, CASQ1, and ADCY8, further regulates its cellular functions, including SOCE activity. Additionally, STIM1 has been implicated in enamel formation and undergoes conformational changes facilitated by interactions with STIMATE. These dynamic interactions highlight the multifaceted role of STIM1 in cellular Ca(2+) signaling and homeostasis.

Stromal interaction molecule 1; STIM1; GOK

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.