| Host: | Rabbit |
| Applications: | WB |
| Reactivity: | Human/Mouse |
| Note: | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: | Rabbit polyclonal antibody anti-Cytosolic carboxypeptidase 4 (723-773 aa) is suitable for use in Western Blot research applications. |
| Clonality: | Polyclonal |
| Conjugation: | Unconjugated |
| Isotype: | IgG |
| Formulation: | Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide. |
| Purification: | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. |
| Concentration: | 1 mg/mL |
| Dilution Range: | WB 1:500-2000 |
| Storage Instruction: | Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
| Gene Symbol: | AGBL1 |
| Gene ID: | 123624 |
| Uniprot ID: | CBPC4_HUMAN |
| Immunogen Region: | 723-773 aa |
| Specificity: | This antibody detects endogenous levels of CBPC4 at Human/Mouse |
| Immunogen: | Synthesized peptide derived from the human CBPC4 at the amino acid range 723-773 |
| Function | Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK. |
| Protein Name | Cytosolic Carboxypeptidase 4 Atp/Gtp-Binding Protein-Like 1 Protein Deglutamylase Ccp4 |
| Database Links | Reactome: R-HSA-8955332 |
| Cellular Localisation | Cytoplasm Cytosol |
| Alternative Antibody Names | Anti-Cytosolic Carboxypeptidase 4 antibody Anti-Atp/Gtp-Binding Protein-Like 1 antibody Anti-Protein Deglutamylase Ccp4 antibody Anti-AGBL1 antibody Anti-CCP4 antibody |
Information sourced from Uniprot.org
