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Merck

S6072

Sigma-Aldrich

Anti-STIM1 (N-terminal) antibody produced in rabbit

enhanced validation

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

Sinónimos:

Anti-GOK, Anti-Stromal interaction molecule I

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100 μL
MXP 10,416.00
200 μL
MXP 13,442.00

MXP 10,416.00


Fecha estimada de envío12 de abril de 2025


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100 μL
MXP 10,416.00
200 μL
MXP 13,442.00

About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

MXP 10,416.00


Fecha estimada de envío12 de abril de 2025


Solicitar un pedido a granel

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 90 kDa

species reactivity

rat, mouse, human

enhanced validation

independent
Learn more about Antibody Enhanced Validation

concentration

~1 mg/mL

technique(s)

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.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Immunogen

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.

application

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

Biochem/physiol Actions

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).

Physical form

Solution in 0.01 M phosphate buffered saline, 7.4 pH, 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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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STIM1 is a Ca 2+ sensor that activates CRAC channels and migrates from the Ca 2+ store to the plasma membrane
Zhang SL, et al.
Nature, 437(7060), 902-902 (2005)
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
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

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