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S8572

Sigma-Aldrich

Anti-STIM2 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-stromal interaction molecule 2

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~100 kDa

species reactivity

human, mouse, rat

concentration

~1.0 mg/mL

technique(s)

western blot: 0.1-0.2 μg/mL using whole extract of mouse brain
western blot: 0.5-1.0 μg/mL using rat brain
western blot: 0.5-1.0 μg/mL using whole extracts of human U87 cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... STIM2(57620)
mouse ... Stim2(116873)
rat ... Stim2(117087)

General description

STIM (stromal interaction molecule) proteins are conserved single-pass transmembrane protein. The three STIM proteins, STIM1, STIM2 and D-Stim, are ubiquitously expressed proteins composed of a single SAM (sterile α-motif) domain and an unpaired EF hand within the highly conserved extracellular region and coiled-coil domains that are conserved in structure and position within the cytoplasmic region. Significant divergence between these proteins was found only at the extreme C-termini. STIM proteins are modified by phosphorylation and N-linked glycosylation.

Immunogen

synthetic peptide corresponding to amino acids 812-833 of human STIM2, conjugated to KLH. The corresponding sequence is identical in rat and mouse.

Application

Anti-STIM2 antibody produced in rabbit has been used in western blotting.

Biochem/physiol Actions

STIM (stromal interaction molecule) required for the regulation of store-operated Ca2+ influx. Store-operated calcium entry is mediated by Ca2+ release-activated Ca2+ (CRAC) channels, following Ca2+ depletion from the endoplasmic reticulum (ER) stores. This process is crucial for gene transcription, proliferation and cytokine release. STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ entry. STIM2 co-localizes with STIM1 in punctae upon store depletion, and coprecipitates with STIM1 from cell lysates, suggesting that they may play a coordinated role in controlling Ca2+ entry.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Inverse regulation of melanoma growth and migration by O rai1/STIM 2-dependent calcium entry
Stanisz H, et al.
Pigment Cell & Melanoma Research, 27(3), 442-453 (2014)
Biochemical properties and cellular localisation of STIM proteins
Dziadek MA and Johnstone LS
Cell Calcium, 42(2), 123-132 (2007)
Familial Alzheimer?s disease-linked presenilin mutants and intracellular Ca2+ handling: A single-organelle, FRET-based analysis
Greotti E, et al.
Cell Calcium, 79(14), 44-56 (2019)
A calcium-redox feedback loop controls human monocyte immune responses: The role of ORAI Ca2+ channels
Saul S, et al.
Science Signaling, 9(418), ra26-ra26 (2016)
Store-operated Ca2+ entry (SOCE) and purinergic receptor-mediated Ca2+ homeostasis in murine bv2 microglia cells: early cellular responses to ATP-mediated microglia activation
Gilbert DF, et al.
Frontiers in Molecular Neuroscience, 9, 111-111 (2016)

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