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R128

Sigma-Aldrich

Monoclonal Anti-Ryanodine Receptor antibody produced in mouse

clone C3-33, ascites fluid

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Synonym(s):
Anti-CCO, Anti-KDS, Anti-MHS, Anti-MHS1, Anti-PPP1R137, Anti-RYDR, Anti-RYR, Anti-RYR-1, Anti-SKRR
MDL number:
MFCD00282461
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

C3-33, monoclonal

mol wt

antigen ~565 kDa (non-mammalian vertebrates, a doublet at 565 kDa represents the α and β isoforms)

species reactivity

canine, rabbit, rat, chicken, amphibian, guinea pig, mouse, fish, human

concentration

~1 mg/mL

technique(s)

immunohistochemistry (frozen sections): 1 μg/mL using 4% paraformaldehyde-fixed, frozen mouse brain tissue
immunoprecipitation (IP): suitable
western blot (chemiluminescent): 1 μg/mL

isotype

IgG1

UniProt accession no.

P21817

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

rat ... Ryr1(114207) , Ryr2(84025)

General description

RyR1 (ryanodine receptor isoform 1) is a homotetrameric intracellular calcium channel, that is present in skeletal muscle tissue. It is located on human chromosome 19q13.1. In rats, RyR1 and RyR2 are expressed in PASMCs (pulmonary artery smooth muscle cells).

Specificity

The antibody reacts strongly with RyR-2 (expressed predominantly in the heart muscle, but also found in stomach, endothelial cells and diffuse areas of the brain; also known as the β isoform), and weakly with RyR-1 (expressed predominantly in skeletal muscle and areas of the brain; also known as the α isoform). It reacts with ryanodine receptor in cardiac muscle of canine, rat, finch and pigeon; in visceral smooth muscle of toad; and in rat brain. It reacts with skeletal muscle of fish and the β isoform of frog, but only weakly with skeletal muscle in rabbit and the α isoform of frog. In immunohistochemistry, the antibody stains are consistent with the endoplasmic reticulum localization of the receptor in the hippocampus.

Immunogen

dog cardiac ryanodine receptors (RyR)

Application

Anti-Ryanodine Receptor has been used in immunofluorescence assay.

Biochem/physiol Actions

In rats PASMCs (pulmonary artery smooth muscle cells), RyR2 (ryanodine receptor isoform 1) participates in RyR-gated Ca2+ entry. It controls the secretion of insulin and glucose homeostasis. After hemorrhagic shock, RyR2 involves in the progress of vascular bi-phasic reactivity to NE (norepinephrine). In human, RyR1 plays an important role in muscle contraction. RYR1 mutation causes CCD (central core disease) and MHS (malignant hyperthermia susceptibility).

Physical form

Containing PBS and 0.05% 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.

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Imaging Ca2+ nanosparks in heart with a new targeted biosensor
Shang W, et al.
Circulation Research, 114(3), 412-420 (2014)
Conformation of ryanodine receptor-2 gates store-operated calcium entry in rat pulmonary arterial myocytes
Lin AH, et al.
Cardiovascular Research, 111(1), 94-104 (2016)
Glucose-Dependent Insulin Secretion in Pancreatic ?-Cell Islets from Male Rats Requires Ca2+ Release via ROS-Stimulated Ryanodine Receptors
Llanos P, et al.
PLoS ONE, 10(6) (2015)
Wei Shang et al.
Circulation research, 114(3), 412-420 (2013-11-22)
In cardiac dyads, junctional Ca2+ directly controls the gating of the ryanodine receptors (RyRs), and is itself dominated by RyR-mediated Ca2+ release from the sarcoplasmic reticulum. Existing probes do not report such local Ca2+ signals because of probe diffusion, so
Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
Samso M, et al.
Nature Structural and Molecular Biology, 12(6), 539-544 (2005)
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