Host: | Rabbit |
Applications: | WB/ELISA/IHC |
Reactivity: | Human/Mouse/Rat |
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-E3 ubiquitin-protein ligase RNF130 (231-280 aa) is suitable for use in Western Blot, ELISA and Immunohistochemistry 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 1:500-2000IHC-P 1:50-300ELISA 2000-20000 |
Storage Instruction: | Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
Gene Symbol: | RNF130 |
Gene ID: | 55819 |
Uniprot ID: | GOLI_HUMAN |
Immunogen Region: | 231-280 aa |
Specificity: | RNF130 Polyclonal Antibody detects endogenous levels of RNF130 protein. |
Immunogen: | The antiserum was produced against synthesized peptide derived from the human RNF130 at the amino acid range 231-280 |
Post Translational Modifications | In vivo measurements suggest this protein is glycosylated. In contrast, in vitro experiments failed to detect glycosylation. |
Function | May have a role during the programmed cell death of hematopoietic cells. Acts as an E3 ubiquitin-protein ligase. |
Protein Name | E3 Ubiquitin-Protein Ligase Rnf130Goliath HomologH-GoliathRing Finger Protein 130Ring-Type E3 Ubiquitin Transferase Rnf130 |
Database Links | Reactome: R-HSA-983168 |
Cellular Localisation | MembraneSingle-Pass Type I Membrane ProteinCytoplasm |
Alternative Antibody Names | Anti-E3 Ubiquitin-Protein Ligase Rnf130 antibodyAnti-Goliath Homolog antibodyAnti-H-Goliath antibodyAnti-Ring Finger Protein 130 antibodyAnti-Ring-Type E3 Ubiquitin Transferase Rnf130 antibodyAnti-RNF130 antibody |
Information sourced from Uniprot.org