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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

CAND1 Antibody #7433

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Filter:
  • WB
  • IP
Western Blotting Image 1: CAND1 Antibody
Western blot analysis of extracts from various cell lines using CAND1 Antibody.
This product is discontinued

Inquiry Info. # 7433

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Supporting Data

REACTIVITY H M R Mk
SENSITIVITY Endogenous
MW (kDa) 130
SOURCE Rabbit
Application Key:
  • WB-Western Blotting 
  • IP-Immunoprecipitation 
Species Cross-Reactivity Key:
  • H-Human 
  • M-Mouse 
  • R-Rat 
  • Mk-Monkey 

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000
Immunoprecipitation 1:50

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

CAND1 Antibody recognizes endogenous levels of total CAND1 protein. This antibody may cross-react with CAND2.

Species Reactivity:

Human, Mouse, Rat, Monkey

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Bovine, Dog

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asn610 of human CAND1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Background

Cullin-associated and neddylation-dissociated (CAND1)/TIP120A is a protein containing multiple HEAT repeats. It functions, in part, as an inhibitor of multiple cullin-RING ubiquitin ligases (CRLs) via binding to cullin-RBX complexes that are both unconjugated to NEDD8 and lack association with substrate recognition subunits (1-3). Indeed, CAND1 has been shown to bind all cullin family members in human cells and analysis of the crystal structure of human CAND1 bound to the CUL1-RBX1 complex suggests that CAND1 inhibits the activity of CRLs by sterically blocking both the substrate recognition subunit binding site and the NEDD8 conjugation site (1,3,4). Conversely, CAND1 binding to cullin-RBX complexes is incompatible with neddylation as NEDD8 conjugated to cullins blocks CAND1 binding, suggesting that CAND1 binds to cullins only after the COP9 signalosome has catalyzed cullin deneddylation. Through its ability to negatively regulate CRL assembly, CAND1 plays an integral part in facilitating CRL activation cycles that allow CRLs to utilize distinct substrate recognition subunits and protects these subunits from undergoing ubiquitin-dependent degradation (5-7).
For Research Use Only. Not For Use In Diagnostic Procedures.
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