Immunohistochemistry analysis of CUL-2 showing staining in the cytoplasm and nucleus of paraffin-embedded human ovarian carcinoma (right) compared to a negative control without primary antibody (left). To expose target proteins, antigen retrieval was performed using 10 mM sodium citrate (pH 6.0), microwaved for 8-15 min. Following antigen retrieval, tissues were blocked in 3% H2O2-methanol for 15 min at room temperature, washed with ddH2O and PBS, and then probed with a CUL-2 Rabbit Polyclonal antibody (511800) diluted in 3% BSA-PBS at a dilution of 1:20 overnight at 4°C in a humidified chamber. Tissues were washed extensively in PBST and detection was performed using an HRP-conjugated secondary antibody followed by colorimetric detection using a DAB kit. Tissues were counterstained with hematoxylin and dehydrated with ethanol and xylene to prep for mounting.
|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Insect, Human, Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic peptide derived from the C-terminus of the human CUL2|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7.4|
|Contains||0.1% sodium azide|
|Tested Applications||Dilution *|
|ELISA (ELISA)||0.1-1.0 ug/ml|
|Flow Cytometry (Flow)||3-5 µg/million cells|
|Immunohistochemistry (Paraffin) (IHC (P))||1:10-1:50|
|Immunoprecipitation (IP)||2-3 µg/ml|
|Western Blot (WB)||1:250-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
CUL-2 is a member of the family of human cullin genes (CUL-1, -2, -3, -4a, -4b, and -5), homologous to the S. cerevisiae cdc53 gene. CUL-1 forms a complex with human p19skp1 and F box protein p45skp2. Together with cdc53 (Known as CulA), as three subunits, they form a ubiquitin ligase controlling proteolysis of G1 cell cycle regulatory proteins. In contrast to CUL-1, CUL-2 does not associate with p19skp1 and p45skp2. Instead, CUL-2 forms a complex with an inactive transcriptional elongation complex, SIII, formed by three subunits: Elongain C, Elongin B and VHL. The function of this association remains unknown.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
|Not Applicable||Not Cited||
Structural and kinetic analysis of the COP9-Signalosome activation and the cullin-RING ubiquitin ligase deneddylation cycle.
51-1800 was used in western blot to study the cullin-RING ubiquitin ligase deneddylation cycle and COP9-signalosome activation by structural and kinetic analysis
|Mosadeghi R,Reichermeier KM,Winkler M,Schreiber A,Reitsma JM,Zhang Y,Stengel F,Cao J,Kim M,Sweredoski MJ,Hess S,Leitner A,Aebersold R,Peter M,Deshaies RJ,Enchev RI||eLife (5:null)||2016|
Ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase Skp1-cullin-F-box ligase (SCF) interact through multiple conformations.
51-1800 was used in western blot to study the interaction between ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase Skp1-cullin-F-box ligase.
|Sandoval D,Hill S,Ziemba A,Lewis S,Kuhlman B,Kleiger G||The Journal of biological chemistry (290:1106)||2015|
|Insect||Not Cited||UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1¿ accumulation.||Bandau S,Knebel A,Gage ZO,Wood NT,Alexandru G||BMC biology (10:null)||2012|
NEDD8 links cullin-RING ubiquitin ligase function to the p97 pathway.
51-1800 was used in western blot to show that NEDD8 links CRL ubiquitin ligase function to the p97 pathway.
|den Besten W,Verma R,Kleiger G,Oania RS,Deshaies RJ||Nature structural and molecular biology (19:511)||2012|
Characterization of the role of COP9 signalosome in regulating cullin E3 ubiquitin ligase activity.
51-1800 was used in western blot to elucidate the mechanism through which COP9 signalosome promotes cullin RING ligase activity in vivo.
|Choo YY,Boh BK,Lou JJ,Eng J,Leck YC,Anders B,Smith PG,Hagen T||Molecular biology of the cell (22:4706)||2011|
|Human||Not Cited||COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.||Mao X,Gluck N,Chen B,Starokadomskyy P,Li H,Maine GN,Burstein E||The Journal of biological chemistry (286:32355)||2011|
Neddylation-induced conformational control regulates cullin RING ligase activity in vivo.
51-1800 was used in western blot to study the effect of neddylation on Cul2 and Cul3 structure.
|Boh BK,Smith PG,Hagen T||Journal of molecular biology (409:136)||2011|
|Human||Not Cited||Renal cell carcinoma risk in type 2 von Hippel-Lindau disease correlates with defects in pVHL stability and HIF-1alpha interactions.||Knauth K,Bex C,Jemth P,Buchberger A||Oncogene (25:370)||2006|
|Human||Not Cited||Tumor suppression by the von Hippel-Lindau protein requires phosphorylation of the acidic domain.||Lolkema MP,Gervais ML,Snijckers CM,Hill RP,Giles RH,Voest EE,Ohh M||The Journal of biological chemistry (280:22205)||2005|
||COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.||Mao X,Gluck N,Chen B,Starokadomskyy P,Li H,Maine GN,Burstein E||The Journal of biological chemistry (286:32355)||2011|
||Renal cell carcinoma risk in type 2 von Hippel-Lindau disease correlates with defects in pVHL stability and HIF-1alpha interactions.||Knauth K,Bex C,Jemth P,Buchberger A||Oncogene (25:370)||2006|