IP3 receptor Antibody [N14P12] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000-1:10000 IP1:30 IHC1:1000

Application
WB, IP, IHC

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
314 kDa 270 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human cerebellum tissue; Mouse cerebellum tissue; Mouse brain; Human brain tissue; Rat brain; HAP1 cells; SH-SY5Y cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
IP3 receptor Antibody [N14P12] detects endogenous levels of total IP3 receptor protein.

Clone
N14P12

Synonym(s)
INSP3R1; ITPR1; IP3 receptor isoform 1; IP3R 1; InsP3R1; Type 1 InsP3 receptor

Background
The IP3 receptor, or IP3R, is a tetrameric ligand-gated calcium channel belonging to the intracellular calcium release channel superfamily and is closely related to ryanodine receptors. It is predominantly located in the endoplasmic reticulum membrane of both excitable and non-excitable cells, where it mediates calcium release in response to inositol 1,4,5-trisphosphate, a process that is essential for cellular signal transduction. Each monomer of about three hundred thirteen kilodaltons consists of an N-terminal IP3-binding core made up of alpha and beta clam-shell domains that clamp IP3's four and five phosphates through arginine, lysine, threonine, and serine residues, a suppressor domain with a hot-spot loop facilitating intersubunit contacts, a central linker and transmembrane domain containing six transmembrane helices that form the channel pore and selectivity filter, and a C-terminal channel-forming domain that includes a cytosolic regulatory region with binding sites for calcium, ATP, and calmodulin. There are three isoforms, IP3R1 through IP3R3, which differ in their sensitivity to inositol trisphosphate and calcium. The primary function of IP3R is to bind IP3 at the binding core, triggering partial domain closure and a conformational change that propagates through the central linker to open the channel pore, allowing calcium efflux from the endoplasmic reticulum into the cytosol. This calcium release generates cytosolic calcium waves, puffs, and oscillations, which are further amplified by calcium-induced calcium release through a low-affinity activating site, following a bell-shaped dose-response curve due to a separate inhibitory site, while ATP binding enhances the open probability of the channel. IP3Rs are central to orchestrating calcium signals that drive muscle contraction, neurotransmitter and glandular secretion, T-cell activation, fertilization, cell proliferation, differentiation, autophagy, and apoptosis, integrating signals from phospholipase C-coupled G protein-coupled receptor pathways. Dysregulation of IP3R function is linked to diseases such as Alzheimer’s disease, where amyloid beta causes hyperactivity, cardiac arrhythmias, and cancer.

Background

The IP3 receptor, or IP3R, is a tetrameric ligand-gated calcium channel belonging to the intracellular calcium release channel superfamily and is closely related to ryanodine receptors. It is predominantly located in the endoplasmic reticulum membrane of both excitable and non-excitable cells, where it mediates calcium release in response to inositol 1,4,5-trisphosphate, a process that is essential for cellular signal transduction. Each monomer of about three hundred thirteen kilodaltons consists of an N-terminal IP3-binding core made up of alpha and beta clam-shell domains that clamp IP3's four and five phosphates through arginine, lysine, threonine, and serine residues, a suppressor domain with a hot-spot loop facilitating intersubunit contacts, a central linker and transmembrane domain containing six transmembrane helices that form the channel pore and selectivity filter, and a C-terminal channel-forming domain that includes a cytosolic regulatory region with binding sites for calcium, ATP, and calmodulin. There are three isoforms, IP3R1 through IP3R3, which differ in their sensitivity to inositol trisphosphate and calcium. The primary function of IP3R is to bind IP3 at the binding core, triggering partial domain closure and a conformational change that propagates through the central linker to open the channel pore, allowing calcium efflux from the endoplasmic reticulum into the cytosol. This calcium release generates cytosolic calcium waves, puffs, and oscillations, which are further amplified by calcium-induced calcium release through a low-affinity activating site, following a bell-shaped dose-response curve due to a separate inhibitory site, while ATP binding enhances the open probability of the channel. IP3Rs are central to orchestrating calcium signals that drive muscle contraction, neurotransmitter and glandular secretion, T-cell activation, fertilization, cell proliferation, differentiation, autophagy, and apoptosis, integrating signals from phospholipase C-coupled G protein-coupled receptor pathways. Dysregulation of IP3R function is linked to diseases such as Alzheimer’s disease, where amyloid beta causes hyperactivity, cardiac arrhythmias, and cancer.

References
https://pubmed.ncbi.nlm.nih.gov/30013099/ https://pubmed.ncbi.nlm.nih.gov/30745293/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%