Product nameAnti-CBL (phospho S669) antibody [EPR2226(2)] - BSA and Azide free
See all CBL primary antibodies
DescriptionRabbit monoclonal [EPR2226(2)] to CBL (phospho S669) - BSA and Azide free
This antibody only detects Cbl phosphorylated at Serine 669.
Tested applicationsSuitable for: WBmore details
Unsuitable for: Flow Cyt,ICC,IHC-P or IP
Species reactivityReacts with: Mouse, Rat, Human
Synthetic peptide within Human CBL (phospho S669). The exact sequence is proprietary.
Ab247648 is the carrier-free version of ab108364. This format is designed for use in antibody labeling, including fluorochromes, metal isotopes, oligonucleotides, enzymes.
Our carrier-free formats are supplied in a buffer free of BSA, sodium azide and glycerol for higher conjugation efficiency.
Use our conjugation kits for antibody conjugates that are ready-to-use in as little as 20 minutes with <1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
ab247648 is compatible with the Maxpar® Antibody Labeling Kit from Fluidigm.
Maxpar® is a trademark of Fluidigm Canada Inc.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMab® patents.
This product is a recombinant rabbit monoclonal antibody.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferConstituent: PBS
Concentration information loading...
- Cell Biology
- Proteolysis / Ubiquitin
- Proteasome / Ubiquitin
- Ubiquitin E3 Enzymes
- RING Finger E3 Ligase
- Signal Transduction
- Signaling Pathway
- Nuclear Signaling
- Nuclear Hormone Receptors
- Epigenetics and Nuclear Signaling
- Nuclear Signaling Pathways
- Nuclear Receptors
Our Abpromise guarantee covers the use of ab247648 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||Use at an assay dependent concentration. Predicted molecular weight: 100 kDa.|
FunctionParticipates in signal transduction in hematopoietic cells. Adapter protein that functions as a negative regulator of many signaling pathways that start from receptors at the cell surface. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including PDGFA, EGF and CSF1, and terminates signaling.
PathwayProtein modification; protein ubiquitination.
Involvement in diseaseDefects in CBL are the cause of Noonan syndrome-like disorder (NSL) [MIM:613563]. NSL is a syndrome characterized by a phenotype reminiscent of Noonan syndrome. Clinical features are highly variable, including facial dysmorphism, short neck, developmental delay, hyperextensible joints and thorax abnormalities with widely spaced nipples. The facial features consist of triangular face with hypertelorism, large low-set ears, ptosis, and flat nasal bridge. Some patients manifest cardiac defects.
Sequence similaritiesContains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain.
Contains 1 RING-type zinc finger.
Contains 1 UBA domain.
DomainThe RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
modificationsPhosphorylated on tyrosine residues by EGFR, SYK, FYN and ZAP70 (By similarity). Phosphorylated on tyrosine residues by INSR.
- Information by UniProt
- 4732447J05Rik antibody
- C CBL antibody
- Cas Br M (murine) ecotropic retroviral transforming sequence antibody
ab247648 has not yet been referenced specifically in any publications.