SP100 Antibody - #DF4247
Product: | SP100 Antibody |
Catalog: | DF4247 |
Description: | Rabbit polyclonal antibody to SP100 |
Application: | WB IHC IF/ICC |
Reactivity: | Human |
Mol.Wt.: | 0 KD; 100kD(Calculated). |
Uniprot: | P23497 |
RRID: | AB_2836598 |
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Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# DF4247, RRID:AB_2836598.
Fold/Unfold
DKFZp686E07254; FLJ00340; FLJ34579; Lysp100b; Nuclear antigen Sp100; Nuclear autoantigen Sp 100; Nuclear autoantigen Sp-100; Nuclear autoantigen Sp100; Nuclear dot associated Sp100 protein; Nuclear dot-associated Sp100 protein; SP 100; SP100; SP100 HMG nuclear autoantigen; SP100 nuclear antigen; SP100_HUMAN; Speckled 100 kDa;
Immunogens
Widely expressed. Sp100-B is expressed only in spleen, tonsil, thymus, mature B-cell line and some T-cell line, but not in brain, liver, muscle or non-lymphoid cell lines.
- P23497 SP100_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQRMFTEDQGVDDRLLYDIVFKHFKRNKVEISNAIKKTFPFLEGLRDRDLITNKMFEDSQDSCRNLVPVQRVVYNVLSELEKTFNLPVLEALFSDVNMQEYPDLIHIYKGFENVIHDKLPLQESEEEEREERSGLQLSLEQGTGENSFRSLTWPPSGSPSHAGTTPPENGLSEHPCETEQINAKRKDTTSDKDDSLGSQQTNEQCAQKAEPTESCEQIAVQVNNGDAGREMPCPLPCDEESPEAELHNHGIQINSCSVRLVDIKKEKPFSNSKVECQAQARTHHNQASDIIVISSEDSEGSTDVDEPLEVFISAPRSEPVINNDNPLESNDEKEGQEATCSRPQIVPEPMDFRKLSTFRESFKKRVIGQDHDFSESSEEEAPAEASSGALRSKHGEKAPMTSRSTSTWRIPSRKRRFSSSDFSDLSNGEELQETCSSSLRRGSGSQPQEPENKKCSCVMCFPKGVPRSQEARTESSQASDMMDTMDVENNSTLEKHSGKRRKKRRHRSKVNGLQRGRKKDRPRKHLTLNNKVQKKRWQQRGRKANTRPLKRRRKRGPRIPKDENINFKQSELPVTCGEVKGTLYKERFKQGTSKKCIQSEDKKWFTPREFEIEGDRGASKNWKLSIRCGGYTLKVLMENKFLPEPPSTRKKRILESHNNTLVDPCEEHKKKNPDASVKFSEFLKKCSETWKTIFAKEKGKFEDMAKADKAHYEREMKTYIPPKGEKKKKFKDPNAPKRPPLAFFLFCSEYRPKIKGEHPGLSIDDVVKKLAGMWNNTAAADKQFYEKKAAKLKEKYKKDIAAYRAKGKPNSAKKRVVKAEKSKKKKEEEEDEEDEQEEENEEDDDK
PTMs - P23497 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
A2 | Acetylation | Uniprot | |
S18 | Phosphorylation | Uniprot | |
T39 | Phosphorylation | Uniprot | |
Y50 | Phosphorylation | Uniprot | |
K55 | Ubiquitination | Uniprot | |
S65 | Phosphorylation | Uniprot | |
K70 | Ubiquitination | Uniprot | |
K87 | Ubiquitination | Uniprot | |
S92 | Phosphorylation | Uniprot | |
S111 | Phosphorylation | Uniprot | |
K151 | Ubiquitination | Uniprot | |
S157 | Phosphorylation | Uniprot | |
S166 | Phosphorylation | Uniprot | |
S171 | Phosphorylation | Uniprot | |
T176 | Phosphorylation | Uniprot | |
S180 | Phosphorylation | Uniprot | |
S189 | Phosphorylation | Uniprot | |
S191 | Phosphorylation | Uniprot | |
T197 | Phosphorylation | Uniprot | |
T198 | Phosphorylation | Uniprot | |
K217 | Ubiquitination | Uniprot | |
K219 | Ubiquitination | Uniprot | |
T221 | Phosphorylation | Uniprot | |
T222 | Phosphorylation | Uniprot | |
S223 | Phosphorylation | Uniprot | |
K225 | Ubiquitination | Uniprot | |
S228 | Phosphorylation | Uniprot | |
S231 | Phosphorylation | Uniprot | |
T234 | Phosphorylation | Uniprot | |
S247 | Phosphorylation | Uniprot | |
S274 | Phosphorylation | Uniprot | |
K297 | Sumoylation | Uniprot | |
K298 | Ubiquitination | Uniprot | |
K300 | Acetylation | Uniprot | |
K300 | Ubiquitination | Uniprot | |
K306 | Acetylation | Uniprot | |
K306 | Sumoylation | Uniprot | |
K306 | Ubiquitination | Uniprot | |
S327 | Phosphorylation | Uniprot | |
S328 | Phosphorylation | Uniprot | |
S331 | Phosphorylation | Uniprot | |
S334 | Phosphorylation | Uniprot | |
T335 | Phosphorylation | Uniprot | |
S350 | Phosphorylation | Uniprot | |
S362 | Phosphorylation | Uniprot | |
K366 | Sumoylation | Uniprot | |
K366 | Ubiquitination | Uniprot | |
K387 | Sumoylation | Uniprot | |
S389 | Phosphorylation | Uniprot | |
S394 | Phosphorylation | Uniprot | |
K396 | Sumoylation | Uniprot | |
S407 | Phosphorylation | Uniprot | |
S409 | Phosphorylation | Uniprot | |
S410 | Phosphorylation | Uniprot | |
S419 | Phosphorylation | Uniprot | |
K430 | Acetylation | Uniprot | |
K430 | Ubiquitination | Uniprot | |
S445 | Phosphorylation | Uniprot | |
S451 | Phosphorylation | Uniprot | |
S452 | Phosphorylation | Uniprot | |
S453 | Phosphorylation | Uniprot | |
S456 | Phosphorylation | Uniprot | |
S459 | Phosphorylation | Uniprot | |
S476 | Phosphorylation | Uniprot | |
K486 | Acetylation | Uniprot | |
S512 | Phosphorylation | Uniprot | |
S524 | Phosphorylation | Uniprot | |
T525 | Phosphorylation | Uniprot | |
S530 | Phosphorylation | Uniprot | |
K557 | Ubiquitination | Uniprot | |
T560 | Phosphorylation | Uniprot | |
K564 | Ubiquitination | Uniprot | |
K594 | Ubiquitination | Uniprot | |
K601 | Ubiquitination | Uniprot | |
K613 | Ubiquitination | Uniprot | |
K673 | Ubiquitination | Uniprot | |
K731 | Acetylation | Uniprot | |
K733 | Acetylation | Uniprot | |
K733 | Methylation | Uniprot | |
K733 | Ubiquitination | Uniprot | |
K739 | Acetylation | Uniprot | |
K739 | Ubiquitination | Uniprot | |
K750 | Ubiquitination | Uniprot | |
T751 | Phosphorylation | Uniprot | |
Y752 | Phosphorylation | Uniprot | |
K764 | Acetylation | Uniprot | |
K764 | Ubiquitination | Uniprot | |
K786 | Ubiquitination | Uniprot | |
Y818 | Phosphorylation | Uniprot | |
Y836 | Phosphorylation | Uniprot |
Research Backgrounds
Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation.
Sumoylated. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting.
Sumoylated. Sumoylated with SUMO1. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting. Sumoylation may stabilize the interaction with CBX5.
Nucleus. Nucleus>PML body. Cytoplasm.
Note: Differences in the subnuclear localization of the different isoforms seem to exist and may also be cell cycle- and interferon-dependent. Accumulates in the cytoplasm upon FAS activation.
Nucleus.
Note: Forms a reticulate or track-like nuclear pattern with denser concentrations at the nuclear lamina and surrounding the nucleoli, a pattern reminiscent of heterochromatin-rich regions according to PubMed:11313457.
Widely expressed. Sp100-B is expressed only in spleen, tonsil, thymus, mature B-cell line and some T-cell line, but not in brain, liver, muscle or non-lymphoid cell lines.
Homodimer; isoforms are able to heterodimerize. Interacts with members of the HP1 family of nonhistone chromosomal protein, such as CBX5 and CBX3 via the PxVxL motif. Interacts with ETS1; the interaction is direct and modulates ETS1 transcriptional activity. Interacts with the MRN complex which is composed of two heterodimers RAD50/MRE11 associated with a single NBN; recruits the complex to PML-related bodies. Interacts with HIPK2; positively regulates TP53-dependent transcription. Interacts with CASP8AP2; may negatively regulate CASP8AP2 export from the nucleus to the cytoplasm. Interacts with SUMO1P1/SUMO5.
(Microbial infection) Interacts with Epstein-Barr virus EBNA-LP; this interaction is important for EBNA-LP coactivator activity.
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL123; may play a role in infection by the virus.
The HSR domain is important for the nuclear body targeting as well as for the dimerization.
Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.
Research Fields
· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
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