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MABC1037

Sigma-Aldrich

Anti-Sp100 Antibody, clone 2H1.1

clone 2H1.1, from mouse

Synonym(s):

Nuclear autoantigen Sp-100, Nuclear dot-associated Sp100 protein, Speckled 100 kDa

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

2H1.1, monoclonal

species reactivity

human

technique(s)

immunocytochemistry: suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

target post-translational modification

unmodified

Gene Information

human ... SP100(6672)

General description

Nuclear autoantigen Sp-100 (UniProt P23497; also known as Nuclear dot-associated Sp100 protein, Speckled 100 kDa) is encoded by the SP100 gene (Gene ID 6672) in human. The SP100 family genes, including SP100, SP110, SP140 and SP140L, encode highly similar proteins mainly expressed in leukocytes. Interferons (IFNs) and other viral infection-related stimuli induce SP100 family gene expression and mutations of SP100 genes are linked to immune diseases and cancers. SP100 colocalizes with promyelocytic leukemia (PML) protein in nuclear bodies (NBs), also known as nuclear domain 10 (ND10), that function to regulate gene transcription via chromatin-based mechanisms and thereby mediate a variety of cellular functions including senescence, apoptosis, protein degradation, telemere stasbility, and defense against viral infections.

Specificity

Clone 2H1.1 targeted epitope region is present in all seven human Sp100 spliced isoforms reported by UniProt (P23497).

Immunogen

Epitope: Internal (N-terminal half).
GST-tagged recombinant human Sp100 internal fragment.

Application

Anti-Sp100 Antibody, clone 2H1.1 is an antibody against Sp100 for use in Western Blotting, Immunocytochemistry.
Immunocytochemistry Analysis: A 1:500 dilution from a representative lot detected Sp100 nuclear foci in HeLa cells.
Research Category
Apoptosis & Cancer
Research Sub Category
Chromatin Biology

Quality

Evaluated by Western Blotting in HepG2 nuclear extract.

Western Blotting Analysis: 2.0 µg/mL of this antibody detected Sp100 in 10 µg of HepG2 nuclear extract.

Target description

~100/78 kDa observed. 100.3 kDa (isoform Sp100-HMG/SP100HMG/SpAlt-HMG), 53.64 kDa (isoform Sp100-A/SP100A/SP100), 78.43 kDa (isoform Sp100-B/SP100B/SpAlt-212), 101.4 kDa (isoform Sp100-C/SP100C), 52.98 kDa (isoform SpAlt-C), 50.46 kDa (isoform 6), and 49.90 kDa (isoform 7) calculated (with Met1 removed). Uncharacterized band(s) may appear in some lysates.

Physical form

Format: Purified
Protein G purified.
Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

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.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Philipp E Merkl et al.
mBio, 10(1) (2019-01-24)
Several host cell nuclear factors are known to restrict herpes simplex virus 1 (HSV-1) replication, but their mechanisms of action remain to be defined. Interferon-inducible protein 16 (IFI16) and the nuclear domain 10-associated proteins, such as promyelocytic leukemia (PML) protein
Dai Wang et al.
Proceedings of the National Academy of Sciences of the United States of America, 104(50), 20037-20042 (2007-12-14)
Human cytomegalovirus infects multiple cell types, including fibroblasts and epithelial cells. It penetrates fibroblasts by fusion at the cell surface but is endocytosed into epithelial cells. In this report, we demonstrate by electron microscopy that the virus uses two different

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