Anti-Proteasome 19S S7 antibody
| Name | Anti-Proteasome 19S S7 antibody |
|---|---|
| Supplier | Abcam |
| Catalog | ab3322 |
| Prices | $384.00 |
| Sizes | 100 µl |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Applications | WB IP ICC/IF ICC/IF |
| Species Reactivities | Human |
| Antigen | Other Immunogen Type corresponding to Human Proteasome 19S S7 |
| Description | Rabbit Polyclonal |
| Gene | PSMC2 |
| Conjugate | Unconjugated |
| Supplier Page | Shop |
Product images
Western blot of proteasome 19S subunit S7 on HeLa cell lysate using ab3322.
ab3322 staining Proteasome 19S S7 in mock transfected rat primary neurons by Immunocytochemistry/ Immunofluorescence. Primary cultures of rat hippocampal neurons were prepared from E18 rats. Cells were fixed in 4% paraformaldehyde and incubated with primary antibody at 1/1000 dilution. The image show red staining with ab3322, nucleus was stained blue with Hoechst H33258 and right image show merged images. The green color seen in image is the GFP staining in similar experiment.
Product References
Nonproteolytic roles of 19S ATPases in transcription of CIITApIV genes. - Nonproteolytic roles of 19S ATPases in transcription of CIITApIV genes.
Maganti N, Moody TD, Truax AD, Thakkar M, Spring AM, Germann MW, Greer SF. PLoS One. 2014 Mar 13;9(3):e91200.
Fusion-related host proteins are actively regulated by NA during influenza - Fusion-related host proteins are actively regulated by NA during influenza
Sui Z, Wen B, Gao Z, Chen Q. PLoS One. 2014 Aug 25;9(8):e105947.
Competition between sumoylation and ubiquitination of serine - Competition between sumoylation and ubiquitination of serine
Anderson DD, Eom JY, Stover PJ. J Biol Chem. 2012 Feb 10;287(7):4790-9.
Ligand-dependent degradation of SRC-1 is pivotal for progesterone receptor - Ligand-dependent degradation of SRC-1 is pivotal for progesterone receptor
Amazit L, Roseau A, Khan JA, Chauchereau A, Tyagi RK, Loosfelt H, Leclerc P, Lombes M, Guiochon-Mantel A. Mol Endocrinol. 2011 Mar;25(3):394-408.
Misfolding of proteins with a polyglutamine expansion is facilitated by - Misfolding of proteins with a polyglutamine expansion is facilitated by
Rousseau E, Kojima R, Hoffner G, Djian P, Bertolotti A. J Biol Chem. 2009 Jan 16;284(3):1917-29.