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Merck
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Documenti fondamentali

S6072

Sigma-Aldrich

Anti-STIM1 (N-terminal)

enhanced validation

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Anti-GOK, Anti-Stromal interaction molecule I

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

PM

antigen 90 kDa

Reattività contro le specie

rat, mouse, human

Convalida avanzata

independent
Learn more about Antibody Enhanced Validation

Concentrazione

~1 mg/mL

tecniche

immunoprecipitation (IP): 2.5-5 μg using extracts of rat PC12 cells.
indirect immunofluorescence: 5-10 μg/mL using human HeLa cells.
western blot: 2-4 μg/mL using whole extract of mouse 3T3 cells.

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... STIM1(6786)
mouse ... Stim1(20866)
rat ... Stim1(117086)

Descrizione generale

STIM1 (stromal interaction molecule 1) is a conserved single-pass transmembrane protein, which is expressed ubiquitously in a wide variety of human primary and transformed cell types. STIM1 is modified by phosphorylation and N-linked glycosylation. STIM1 localized predominantly in the membrane of the endoplasmic reticulum (ER). It contains an N-terminal EF hand motif located in the ER lumen and appears to function as a sensor of ER Ca2+ levels.

Immunogeno

synthetic peptide corresponding to amino acids 61-74 of human STIM1, conjugated to KLH via a C-terminal cysteine residue. The corresponding sequence is identical in rat and mouse.

Applicazioni

Anti-STIM1 (N-terminal) antibody produced in rabbit has been used in:
  • western blotting
  • immunoprecipitation
  • immunofluorescence

Azioni biochim/fisiol

STIM1 (stromal interaction molecule 1) is required for the activation of store-operated Ca2+ influx. Overexpression of STIM1 and Orai1 markedly increases the calcium release-activated calcium (CRAC) current (I-CRAC).

Stato fisico

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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I clienti hanno visto anche

Large store-operated calcium selective currents due to co-expression of Orai1 or Orai2 with the intracellular calcium sensor, Stim1
Mercer JC, et al.
The Journal of Biological Chemistry, 281(34), 24979-24990 (2006)
Identification and characterization of the STIM (stromal interaction molecule) gene family: coding for a novel class of transmembrane proteins
Williams RT, et al.
The Biochemical Journal, 357(3), 673-685 (2001)
Vivek Krishnan et al.
eLife, 11 (2022-02-12)
Peripheral coupling between the sarcoplasmic reticulum (SR) and plasma membrane (PM) forms signaling complexes that regulate the membrane potential and contractility of vascular smooth muscle cells (VSMCs). The mechanisms responsible for these membrane interactions are poorly understood. In many cells
Inhibition of store-operated calcium entry attenuates MPP+-induced oxidative stress via preservation of mitochondrial function in PC12 cells: involvement of Homer1a
Li X, et al.
PLoS ONE, 8(12), e83638-e83638 (2013)
Alicia Sampieri et al.
Scientific reports, 8(1), 13252-13252 (2018-09-07)
The involvement of inositol trisphosphate receptor (IP3R) in modulating store-operated calcium entry (SOCE) was established many years ago. Nevertheless, the molecular mechanism responsible for this observation has not been elucidated to this date. In the present study we show that

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