|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for STIM1(NM_003156.3) Search again
Product ID:
HQP017786
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
D11S4896E, GOK, IMD10, STRMK, TAM, TAM1
Gene Description:
stromal interaction molecule 1
Target Gene Accession:
NM_003156.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
|
|
| A | B |
|
Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
|
Summary
This gene encodes a type 1 transmembrane protein that mediates Ca2+ influx after depletion of intracellular Ca2+ stores by gating of store-operated Ca2+ influx channels (SOCs). It is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocrotical carcinoma, and lung, ovarian, and breast cancer. This gene may play a role in malignancies and disease that involve this region, as well as early hematopoiesis, by mediating attachment to stromal cells. This gene is oriented in a head-to-tail configuration with the ribonucleotide reductase 1 gene (RRM1), with the 3' end of this gene situated 1.6 kb from the 5' end of the RRM1 gene.
Gene References into function
- STIM proteins function as Ca(2+) store sensors in the signaling pathway connecting Ca(2+) store depletion to Ca(2+) influx.
- Increased expression levels of STIM1 correlate with a gain in function of Ca(2+) release-activated Ca(2+) (CRAC) channel activity.
- STIM1 and CRACM1 interact functionally. Overexpression of both proteins greatly potentiates I(CRAC), suggesting that STIM1 and CRACM1 mutually limit store-operated currents and that CRACM1 may be the long-sought CRAC channel.
- suppression of store-operated channels function by Orai1 overexpression likely reflects a required stoichiometry between STIM1 and Orai1
- STIM1 is a required mediator of store-operated channel (SOC) activation and plays a coordinated role with STIM2 in controlling SOC-mediated Ca(2+) entry signals.
- Interaction of STIM1 with endogenously expressed human canonical TRP1 upon depletion of intracellular Ca2+ stores.
- STIM1 is a key regulator of activity rather than a channel component, and reveal similar regulation of SOC, I(crac) and TRPC channel activation by STIM1.
- These studies identify an ER structure underlying store-operated Ca(2+) entry, whose extreme proximity to the PM may enable STIM1 to interact with CRAC channels or associated proteins.
- STIM1 acts as a key signal for store operated calcium channel activation in human airway myocytes.
- STIM1 has a role as an Endoplasmic Reticulum Ca2+ sensor
- Therefore, we propose that store depletion causes aggregation and translocation of STIM1 in close apposition to the plasma membrane.
- in contrast to store-operated channels, regulation of ARC channels by STIM1 depends exclusively on the pool of STIM1 constitutively residing in the plasma membrane
- Ca2+ entry supporting [Ca2+]i oscillations in HEK293 cells depends upon the Ca2+ sensor, Stim1, and calcium release-activated Ca2+ channel protein, Orai1
- dynamic assembly of TRPC1-STIM1-Orai1 ternary complex is involved in activation of SOC channel in response to internal Ca2+ store depletion
- endoplasmic reticulum refilling is largely preserved at reduced STIM1 levels
- peripheral STIM1 relocalization that is causal in regulation of SOCE is determined by the status of [Ca(2+)] in the ER in close proximity to the plasma membrane
- LPA and UTP may exert distinct effects on the duration of STIM1 localization at the plasma membrane, and thus, on the magnitude and duration of agonist-induced calcium entry
- analysis of STIM1 surface exposure by fluorescent imaging with a hexahistidine-Zn2+-dye
- We propose a new definition of SOCs, as channels that are regulated by STIM1 and require the store depletion-mediated clustering of STIM1. By this definition, all TRPC channels, except TRPC7, function as SOCs.
- STIM1 oligomers translocate on average only 2 mum to reach endoplasmic reticulum-plasma membrane junctions
- analysis of the plasma membrane-endoplasmic reticulum contact sites reveals the presence of additional molecular components within the STIM1-Orai1 Complex
- the interacting domains of STIM1 and Orai1 have roles in Ca2+ release-activated Ca2+ channel activation
- Data suggest that microtubules play a facilitative role in the store-operated Ca(2+) entry signaling pathway by optimizing the localization of STIM1.
- Our biophysical studies reveal a structural stability difference in the EF-SAM region between STIM1 and STIM2, which may account for their different biological functions.
- C-terminal coiled-coil motif of ORAI1 represents a key domain for dynamic coupling to STIM1.
- Orai1-STIM1 protein complex is one of the molecular components involved in Pb2+ entry.
- STIM1 directly binds to the microtubule-plus-end-tracking protein EB1 and forms EB1-dependent comet-like accumulations at the sites where polymerizing microtubule ends come in contact with the ER network.
- results imply a positive feedback loop in which an initial TCR signal favors up-regulation of STIM1 and Orai proteins that would augment Ca2+ signaling during subsequent antigen encounter
- demonstrate a functional requirement for Orai1 in TRPC1+STIM1-dependent SOCE
- Soft substrate up-regulates the interaction of STIM1 with store-operated Ca(2+) channels, which results in the activation of mu-calpain and subsequently induces normal epithelial cell apoptosis.
- The effects of 2-aminoethoxydiphenyl borate on orai1, orai2, orai3 metabolism in HEK293 cells with and without STIM1 are reported.
- Data show that STIM1 and TRPC1 interact and insert TRPC1 into lipid rafts, where TRPC1 functions as a store-operated channel; in the absence of STIM1, TRPC1 associates with other members from the TRPC family of channels to form receptor-operated channels
- intact lipid raft domains determine targeting of STIM1 clusters to ER-plasma membrane junctions following store depletion which facilitates the functional interaction of STIM1 with TRPC1 and activation of store-operated Ca(2+) entry
- analysis of movement of the calcium sensor STIM1 and the calcium channel Orai1 in activated T-cells
- Huh-7 and HepG2 cells (hepatoma cell lines) express transient receptor potential canonical 1 (TRPC1) and TRPC6, as well as STIM1 and Orai1, and these 4 channels are the most likely candidates to account for the store-operated calcium entry in these cells
- ATP depletion induces translocation of STIM1 to puncta and formation of STIM1-ORAI1 clusters: translocation and re-translocation of STIM1 does not require ATP.
- evidence for STIM1:Orai1 as a primary pathway for agonist-evoked Ca2+ influx in the platelet and megakaryocyte.
- plasma membrane STIM1 may play a regulatory role in store-operated channel activation
- the STIM1-Orai1-hTRPC1 complex has a role in the activation of store-operated Ca(2+) entry
- Data challenge the idea of direct conformational coupling between STIM1 and Orai1 as a viable mechanism of puncta formation and SOCE activation and uncover greater complexity in their relationship.
- Dynamic imaging of calcium and STIM1 in the same cell using wide-field TIRF microscopy is reported.
- Report interactions, functions, and independence of plasma membrane STIM1 and TRPC1 in vascular smooth muscle cells.
- identify a STIM1-dependent conformational change in Orai1 during the activation of CRAC channels
- Knockdown of Stim1 inhibits endothelial proliferation and causes cell cycle arrest at S and G2/M phase.
- Structurally critical mutations in the canonical EF-hand, "hidden" EF-hand, or SAM domain disrupt Ca2+ sensitivity in oligomerization via destabilization of the entire EF-SAM entity.
- STIM1 gates TRPC1 by intermolecular electrostatic interaction.
- distinct oligomerization dynamics of STIM isoforms have evolved to adapt to differential roles in Ca(2+) homeostasis and signaling
- Data demonstrate a role for Orai1 and STIM1 in tumor metastasis and suggest store-operated calcium entry channels as potential cancer therapeutic targets.
- Studies establish a molecular mechanism for store-operated Ca(2+) entry in which the direct binding of STIM1 to Orai1 drives the accumulation and the activation of Ca2+ release-activated Ca2+ channels at endoplasmic reticulum-plasma membrane junctions.