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AB268383

Recombinant Human CBL protein (Tagged)

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Recombinant Human CBL protein (Tagged) is a Human Fragment protein, in the 1 to 375 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

CBL2, RNF55, CBL, E3 ubiquitin-protein ligase CBL, Casitas B-lineage lymphoma proto-oncogene, Proto-oncogene c-Cbl, RING finger protein 55, RING-type E3 ubiquitin transferase CBL, Signal transduction protein CBL

1 Images
SDS-PAGE - Recombinant Human CBL protein (Tagged) (AB268383)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human CBL protein (Tagged) (AB268383)

SDS-PAGE analysis of ab268383.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P22681

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.79% Tris HCl, 0.31% Glutathione, 0.29% Sodium chloride, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MAGNVKKSSGAGGGSGSGGSGSGGLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMG","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":375,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P22681","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The CBL protein also known as C-cbl or Casitas B-lineage lymphoma proto-oncogene serves as an E3 ubiquitin-protein ligase. This protein with a molecular mass of approximately 120-130 kDa plays a critical role in the regulation of receptor tyrosine kinases. It facilitates the polyubiquitination of activated receptor proteins targeting them for degradation in the proteasome. CBL is predominantly expressed in various tissues including the hematopoietic system. It is a significant component in the control of cell signaling and helps maintain cellular homeostasis.
Biological function summary

The CBL protein acts as a negative regulator for several signaling pathways. It integrates into signaling complexes and modulates the activation of pathways by interacting with other proteins. CBL does not act alone; it commonly forms complexes with proteins such as Grb2 and p85 influencing downstream signaling influence in pathways. This regulation prevents excessive activation of signals that can lead to cellular proliferation or differentiation abnormally.

Pathways

CBL integrates into the ubiquitin-proteasome system and the Ras signaling pathway. Within these pathways CBL works to modulate cell surface receptors ensuring that signaling threshold is not surpassed. The importance of CBL in the Ras signaling pathway is highlighted by its interactions with proteins like Ras-GAP and SHP2. Through these interactions CBL controls the rate of signal transduction affecting cellular responses such as growth survival and motility.

CBL involvement has been linked to several forms of cancer and immune deficiencies. Mutations or dysregulation of the CBL gene can lead to myelodysplastic syndromes and acute myeloid leukemia. In these conditions the interaction between CBL and other proteins such as JAK2 becomes dysregulated driving abnormal cell growth and survival. Furthermore CBL’s failure to properly degrade tyrosine kinase receptors can contribute to enhanced signaling fostering oncogenic processes.
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Specifications

Form

Liquid

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General info

Function

E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed : 10514377, PubMed : 11896602, PubMed : 14661060, PubMed : 14739300, PubMed : 15190072, PubMed : 17509076, PubMed : 18374639, PubMed : 19689429, PubMed : 21596750, PubMed : 28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed : 10514377, PubMed : 14661060, PubMed : 14739300, PubMed : 17094949, PubMed : 17509076, PubMed : 17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed : 15190072, PubMed : 18374639, PubMed : 21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed : 11896602). Ubiquitinates EGFR and SPRY2 (PubMed : 17094949, PubMed : 17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed : 28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed : 15190072, PubMed : 18374639). Essential for osteoclastic bone resorption (PubMed : 14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed : 14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity).

Post-translational modifications

Phosphorylated on tyrosine residues by ALK, EGFR, SYK, FYN and ZAP70 (By similarity). Phosphorylated on tyrosine residues in response to FLT1 and KIT signaling. Phosphorylated on tyrosine residues by INSR and FGR. Phosphorylated on several tyrosine residues by constitutively activated FGFR3. Not phosphorylated at Tyr-731 by FGFR3. Phosphorylated on tyrosine residues by activated CSF1R, PDGFRA and PDGFRB. Phosphorylated on tyrosine residues by HCK.. Ubiquitinated, leading to its degradation via the proteasome (PubMed:11896602, PubMed:20094046). Ubiquitination is negatively regulated by IFT20 (PubMed:29237719).

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Product protocols

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Target data

E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed : 10514377, PubMed : 11896602, PubMed : 14661060, PubMed : 14739300, PubMed : 15190072, PubMed : 17509076, PubMed : 18374639, PubMed : 19689429, PubMed : 21596750, PubMed : 28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed : 10514377, PubMed : 14661060, PubMed : 14739300, PubMed : 17094949, PubMed : 17509076, PubMed : 17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed : 15190072, PubMed : 18374639, PubMed : 21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed : 11896602). Ubiquitinates EGFR and SPRY2 (PubMed : 17094949, PubMed : 17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed : 28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed : 15190072, PubMed : 18374639). Essential for osteoclastic bone resorption (PubMed : 14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed : 14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity).
See full target information CBL
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