Ugrás a tartalomra
Merck

O4886

Sigma-Aldrich

Monoclonal Anti-Opsin antibody produced in mouse

clone RET-P1, ascites fluid

Szinonimák:

Anti-Opsin Antibody, Mouse Anti-Opsin, Opsin Detection Antibody

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41
konjugátum:
unconjugated
application:
ELISA (i)
EM
ICC
IHC (f)
RIA
WB
klón:
RET-P1, monoclonal
faj reaktivitás:
goldfish, mouse, tiger salamander, rat, amphibian, quail, dove, duck, rabbit, bovine, human, turtle
citations:
54
technika/technikák:
electron microscopy: suitable
immunocytochemistry: suitable using cultured cells
immunohistochemistry (frozen sections): 1:10,000 using frozen sections of rat eye
indirect ELISA: suitable
radioimmunoassay: suitable
western blot: suitable

biológiai forrás

mouse

Minőségi szint

konjugátum

unconjugated

antitest forma

ascites fluid

antitest terméktípus

primary antibodies

klón

RET-P1, monoclonal

molekulatömeg

antigen 39 kDa by immunoblotting (IB of rat retina produces closely spaced doublet)

tartalmaz

15 mM sodium azide

faj reaktivitás

goldfish, mouse, tiger salamander, rat, amphibian, quail, dove, duck, rabbit, bovine, human, turtle

technika/technikák

electron microscopy: suitable
immunocytochemistry: suitable using cultured cells
immunohistochemistry (frozen sections): 1:10,000 using frozen sections of rat eye
indirect ELISA: suitable
radioimmunoassay: suitable
western blot: suitable

izotípus

IgG1

UniProt elérési szám

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... RHO(6010)
mouse ... Rho(212541)
rat ... Rho(24717)

Általános leírás

Mouse monoclonal clone RET-P1 anti-Opsin antibody recognizes an epitope located in amino acid residues 4-10 at the N-terminus of the rhodopsin molecule. In immunoblotting of rat retina, the antibody labels a closely spaced doublet of 39 kDa and less intense bands of 78 and 115 kDa, representing rhodopsin monomer and aggregates. Higher M.W. bands are stained in pituitary (251 and 288 kDa) and in hypothalamus (269 and 331 kDa) in addition to several lower M.W. bands. The product specifically labels the cell bodies, outer and inner segments (rods but not cones) of rat photoreceptor surface. It reacts with bovine, duck, amphibian, goldfish, rabbit, rat, turtle, tiger salamander, mouse, dove, quail, and human rhodopsin/opsin.
Opsin belongs to rhodopsin receptor. The gene is located on human chromosome 3q22.1. Opsin gene is mainly expressed in rod cells.
Photoreceptors are responsible for the initial step in visual processing, converting the signal of photon absorption into synaptic transmission. The visual pigment in vertebrate rods responsible for the absorption of light quanta is rhodopsin (also called opsin). Rhodopsin comprises >95% of the rod outer segments (ROS) intrinsic membrane protein and is a glycoprotein possessing two asparagine-linked oligosaccharide groups at amino acid residues 2 and 15 of the N-terminus. Light is absorbed by rhodopsin and the subsequent conformational change leads to the activation of a cyclic GMP phosphodiesterase through a specific G-protein intermediate, transducin.

Immunogén

rat retinal membranes.

Alkalmazás

Monoclonal Anti-Opsin antibody produced in mouse has been used in immunofluorescence and histology.
Mouse monoclonal clone RET-P1 anti-Opsin antibody is used to tag opsin/rhodopsin for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques such as immunoblotting, immunocytochemistry of cultured cells, immunohistochemistry (paraformaldehyde/glutaraldehyde-fixed, paraformaldehyde perfusion-fixed, frozen sections), immunoelectron microscopy, ELISA, competitive ELISA, and solid phase RIA. It is used as a probe to determine the presence and roles of opsin/rhodopsin in studies of rhodopsin location, functional properties and molecular mechanisms governing rod photoreceptor differentiation.

Biokémiai/fiziológiai hatások

Mutations in rhodopsin gene are linked to retinitis pigmentosa (RP) and congenital night blindness.

Jogi nyilatkozat

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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Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

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


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Az ügyfelek ezeket is megtekintették

Nuclear architecture of rod photoreceptor cells adapts to vision in mammalian evolution
Solovei I, et al.
Cell, 137(2), 356-368 (2009)
Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
Rao VR, et al.
Nature, 367(6464), 639-639 (1994)
Sutisak Kitareewan et al.
International journal of oncology, 33(2), 397-404 (2008-07-19)
All-trans-retinoic acid (RA) treatment of acute promyelocytic leukemia (APL) cases expressing the t(15;17) product, PML/RARalpha, is a successful example of differentiation therapy. Uncovering RA target genes is of considerable interest in APL. This study comprehensively examines in APL cells transcriptional
Sox9 is expressed in mouse multipotent retinal progenitor cells and functions in Muller glial cell development
Poche RA, et al.
The Journal of Comparative Neurology, 510(3), 237-250 (2008)
Autologous transplantation of RPE with partial-thickness choroid after mechanical debridement of Bruch membrane in the rabbit
Hu Y, et al.
Investigative Ophthalmology & Visual Science, 49(7), 3185-3192 (2008)

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