S6072
Anti-STIM1 (N-terminal) 兔抗
~1 mg/mL, affinity isolated antibody, buffered aqueous solution
别名:
Anti-GOK, Anti-Stromal interaction molecule I
产品名称
Anti-STIM1 (N-terminal) 兔抗, ~1 mg/mL, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
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
Quality Level
Gene Information
human ... STIM1(6786)
mouse ... Stim1(20866)
rat ... Stim1(117086)
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).
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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, 7.4 pH, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
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)
Stephen Baine et al.
Journal of cellular and molecular medicine, 25(10), 4637-4648 (2021-03-24)
Heart failure (HF) is characterized by asymmetrical autonomic balance. Treatments to restore parasympathetic activity in human heart failure trials have shown beneficial effects. However, mechanisms of parasympathetic-mediated improvement in cardiac function remain unclear. The present study examined the effects and
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
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)
Mykola Mamenko et al.
Journal of the American Society of Nephrology : JASN, 27(7), 2035-2048 (2015-11-18)
Store-operated calcium entry (SOCE) is the mechanism by which extracellular signals elicit prolonged intracellular calcium elevation to drive changes in fundamental cellular processes. Here, we investigated the role of SOCE in the regulation of renal water reabsorption, using the inbred
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