Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
HighlightsWith deep understanding in antibody-related realms and extensive project experience, Creative Biolabs offers a variety of references to help you learn more about our capacities and achievements, including infographic, flyer, case study, peer-reviewed publications, and all kinds of knowledge that can assist your projects. You are also welcome to contact us directly for more specific solutions.
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Loading...All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.
Structural characteristics and physiological functions: Matrix-interacting molecule 1(STIM1) is encoded by STIM1 gene and belongs to type I endoplasmic reticulum transmembrane sensing protein, which is widely expressed in the lipid bilayer structure of endoplasmic reticulum in various mammalian cells. Compared with the cytosolic soluble signal regulator, STIM1 has unique structural characteristics, with a conservative endoplasmic reticulum cavity calcium sensing function motif and a long cytoplasmic effect domain, and no ion permeable channel, so it can not directly mediate ion transmembrane transport. The protein is mainly located in the endoplasmic reticulum membrane, which can accurately sense the dynamic changes of calcium ion concentration in the endoplasmic reticulum cavity under physiological conditions. When the function of calcium sensing system in endoplasmic reticulum is insufficient, the cytosolic calcium homeostasis is easily broken, and STIM1 can stabilize the calcium pool-dependent calcium signal in different cell microenvironments through signal buffering. Because of the obvious heterogeneity of calcium pool activity in different cells, cells need to rely on a variety of endoplasmic reticulum transmembrane sensing proteins to maintain the overall stability of intracellular calcium signal, in which STIM1 can mediate the interaction between endoplasmic reticulum calcium pool and cell membrane functional molecules through conformational changes and oligomerization reactions, and inhibit abnormal calcium signal conduction, thus maintaining the dynamic balance of intracellular calcium ions.
Mutation effect, regulatory mechanism and research value: STIM1 gene mutation can change the protein's ability to sense calcium ions and its binding characteristics with downstream molecules, resulting in abnormal remodeling of cellular calcium signal response mode. Existing studies have confirmed that among all kinds of sensing proteins located in endoplasmic reticulum, only STIM1 has the dual functions of sensing calcium signal in endoplasmic reticulum cavity and coupling with cell membrane molecules, and no other homologous proteins can replace this biological characteristic at present. The expression level of STIM1 can accurately reflect the functional activity of calcium pool in the endoplasmic reticulum of cells, and it is a key target to study the transmembrane calcium sensing mechanism of endoplasmic reticulum and the regulation signal pathway of calcium pool. At the level of molecular regulation, STIM1 is stably anchored on the endoplasmic reticulum membrane structure, which can respond to the depletion signal of cell calcium pool and then combine with downstream functional molecules, and this process will not trigger continuous signal cascade activation. Different from cytoplasmic free signal molecules, the transmembrane localization of endoplasmic reticulum can simultaneously monitor calcium concentration and regulate protein interaction at the endoplasmic reticulum-cell membrane interface. Once the function of STIM1 is damaged or its expression is down-regulated, the cellular calcium pool-dependent signal transduction will be inhibited, and the buffering and regulating ability of intracellular calcium signals will be significantly reduced, which fully highlights the important academic position and research value of STIM1 in the basic research of endoplasmic reticulum transmembrane sensing proteins.
Fig. 1 Domain organization and partial structural fragments of human STIM1. STIM1 is an ER‑resident type‑I transmembrane calcium sensor, featuring luminal EF‑hand‑SAM calcium‑sensing module and cytosolic coiled‑coil effector domains.1
The biological functions of transmembrane STIM1 sensor protein are focused on sustained luminal calcium perception and inter-membrane signalling coordination:
Creative Biolabs offers purified STIM1 membrane samples produced under unified preparation workflows, including full-length STIM1 constructs and isolated domain-truncated variants. Truncated domain fragments cannot support complete calcium-sensing and partner-coupling behaviours, while full-length constructs suit research focused on ER-luminal calcium perception and inter-membrane protein-partner interaction observation. All batches receive uniform quality screening. Functional relevant observation may only be carried out with full-length samples under simulated ER-membrane microenvironment setups. Consistent structural features are preserved across batches to support comparative laboratory analysis across separate test groups. Full-length STIM1 samples retain intact calcium-sensing and effector-domain conformation after standardized purification, which supports reliable detection of weak and transient protein-partner contacts for comparative functional analysis.
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Creative Biolabs provides adjustable STIM1 expression cell research models with varied expression levels, applicable to structural observation of ER-resident transmembrane calcium sensors and research into inter-membrane protein-partner molecular interaction. Sample evaluation includes sustained target expression detection and preliminary partner-interaction observation, enabling side-by-side comparison of sensor-mediated binding behaviours under differing expression abundances. These cell systems can pair with diverse laboratory analysis schemes to track changes in partner-coupling efficiency alongside shifting target protein levels.
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Anti-STIM1 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for endoplasmic-reticulum membrane localization mapping and identification of multi-protein junction-associated molecular complexes. The antibody series can work alongside common laboratory detection reagents to realize multi-dimensional observation of target distribution within diverse tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for STIM1 research:
STIM1 might act as an ER-resident transmembrane calcium-sensor and participate in luminal calcium perception to couple ER-store status with plasma-membrane molecular partners.
STIM1 expression status could alter store-operated calcium-signal propagation efficiency and intracellular calcium homeostasis, serving as a major regulatory mediator of ER-dependent calcium-signalling biological processes.
No, all STIM1 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material designs and functional tests are optimized exclusively for basic laboratory research scenarios, without matching clinical application standards.
Offerings include full-length STIM1 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on ER calcium-store homeostasis and junction-mediated calcium-signal transmission.
Laboratory observation schemes may include protein-partner interaction related tests to analyse sensor-associated behaviours under simulated ER-membrane environments.
