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Merck

C1862

Anti-Coilin antibody, Mouse monoclonal

~1.5 mg/mL, clone pδ, purified from hybridoma cell culture

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:

Nombre del producto

Anti-Coilin antibody, Mouse monoclonal, ~1.5 mg/mL, clone pδ, purified from hybridoma cell culture

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

pδ, monoclonal

form

buffered aqueous solution

mol wt

antigen ~80 kDa by SDS-PAGE

species reactivity

human

concentration

~1.5 mg/mL

technique(s)

immunocytochemistry: suitable
microarray: suitable
western blot: 1-2 μg/mL using HeLa nuclear extract

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

human ... COIL(8161)

Application

Monoclonal Anti-Coilin antibody produced in mouse has been used in:
  • immunoblotting
  • immunocytochemistry
  • cell microinjection
  • fluorescence imaging
  • indirect immunofluorescence

Biochem/physiol Actions

Mutating Serine-202 to Aspartate causes the disappearance of coiled bodies and a redistribution of coilin to intranucleolar domains. Coilin plays a key role in ribonucleoprotein and Cajal body formation.
The antibody recognizes the C-terminal region of human coilin and does not recognize mouse coilin.

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

Monoclonal Anti-Coilin (mouse IgG1 isotype) is derived from the pδ hybridoma produced by the fusion of mouse myeloma cells and splenocytes from mice immunized with coilin. Coilin contains two nuclear localization sequences (NLS) (at amino acid 107-112 and 181-198) and several serine residues that are phosphorylated in vivo. The description of specific intranuclear structures known today as Cajal bodies was first published in 1903 by the neuro-cytologist Ramon-γ-Cajal who discovered that neurons contained spherical structures of around 0.5 μm in diameter that were often associated with nucleoli, nucleolar accessory bodies. It was found that patients with auto-antibodies against coiled bodies recognize a protein of 80 kDa termed p80-coilin. Nuclear antigens shown to colocalize with p80 coilin in Cajal bodies include basal transcription factors, cell cycle factors (cdks), splicing snRNPs and nucleolar factors including snoRNP.

Immunogen

C-terminal (389 amino acids) human coilin

Physical form

Supplied as a solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

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Clase de almacenamiento

12 - Non Combustible Liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Emmanuelle Querido et al.
STAR protocols, 1(2), 100104-100104 (2020-10-29)
Fluorescent in situ hybridization (FISH) on the RNA moiety of human telomerase (hTR) with 50-mer probes detects hTR RNA accumulated in Cajal bodies. Using both live-cell imaging and single-molecule inexpensive FISH, our published work revealed that only a fraction of
Cell nuclei have lower refractive index and mass density than cytoplasm
Schurmann M, et al.
Journal of Biophotonics, 9(10), 1068-1076 (2016)
Control of Cajal body number is mediated by the coilin C-terminus
Shpargel KB, et al.
Journal of Cell Science, 116(2), 303-312 (2003)
Run-Wen Yao et al.
RNA (New York, N.Y.), 27(6), 725-733 (2021-04-14)
The mammalian cell nucleus contains different types of membrane-less nuclear bodies (NBs) consisting of proteins and RNAs. Microscopic imaging has been widely applied to study the organization and structure of NBs. However, current fixation methods are not optimized for such
Shuntaro Miyake et al.
RNA biology, 19(1), 1244-1255 (2022-11-23)
Intracellular and intercellular signalling networks play an essential role in optimizing cellular homoeostasis and are thought to be partly reflected in nuclear mRNA dynamics. However, the regulation of nuclear mRNA dynamics by intracellular and intercellular signals remains largely unexplored, and

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