Abcam, ab101987, Anti-CAND1 antibody

Size: 100µg
Rabbit Polyclonal CAND1 antibody. Suitable for IHC-P, IP, WB and reacts with Mouse, Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human CAND1 aa 1150 to C-terminus.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Human,
Applications:IHC-P, IP, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human CAND1 aa 1150 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.Q86VP6

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Storage buffer-pH: 7 - 8Preservative: 0.09% Sodium azideConstituents: Tris citrate/phosphate, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
CAND1 also known as cullin-associated and neddylation-dissociated 1 is a scaffolding protein with a molecular mass of approximately 130 kDa. It is found in the cytoplasm and nucleus of eukaryotic cells. CAND1 plays a critical role in regulating the activity of cullin-RING ubiquitin ligases (CRLs) which are important for protein degradation processes. By interacting with neddylated cullin proteins CAND1 modulates the assembly and disassembly of these CRL complexes therefore influencing their activity.
Biological function summary
CAND1 mediates the dynamics of CRL complexes acting as a regulator of substrate specificity and turnover. CAND1 does not function alone; it is integral to a complex that includes cullin proteins and various CRL adaptors. This interaction ensures the right substrates are targeted for ubiquitination leading to proteasomal degradation. The ability of CAND1 to bind to cullin substrates is influenced by cullin neddylation and deneddylation cycles making it essential for the proper function of the ubiquitin-proteasome system.
Pathways
Studies have shown that CAND1 is important in the ubiquitin-proteasome pathway along with the neddylation pathway. Within these pathways it primarily interacts with proteins such as cullins 1 3 and 4 which are central to CRLs. By regulating these interactions CAND1 ensures that protein turnover is controlled which is important for processes like cell cycle progression and signal transduction.
Research suggests a connection between CAND1 dysregulation and certain cancers as well as neurodegenerative disorders. In cancer aberrant regulation of CAND1 can lead to uncontrolled cell proliferation due to faulty protein degradation. In neurodegenerative diseases ineffective CAND1-mediated pathways may contribute to the accumulation of damaged proteins. Understanding CAND1's relationship with key proteins in these conditions such as p53 in cancer highlights its potential as a therapeutic target.