Skip to Content
MilliporeSigma
All Photos(3)

Documents

C1862

Sigma-Aldrich

Anti-Coilin antibody, Mouse monoclonal

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

Sign Into View Organizational & Contract Pricing

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

biological source

mouse

Quality Level

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

Gene Information

human ... COIL(8161)

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.

Specificity

The antibody recognizes the C-terminal region of human coilin and does not recognize mouse coilin.

Immunogen

C-terminal (389 amino acids) human coilin

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.

Physical form

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

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
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
Coilin: The first 25 years
Machyna M, et al.
RNA Biology, 12(6), 590-596 (2015)
P68 RNA helicase (DDX5) alters activity of cis-and trans-acting factors of the alternative splicing of H-Ras
Camats M, et al.
Testing, 3(8), e2926-e2926 (2008)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service