Anti-RFP-Tag antibody [SMM5503] (STJ11107573)
SPECIFICATIONS
ClonalityMonoclonal
HostMouse
ConjugationUnconjugated
IsotypeIgG1
General Information
| Short Description | Mouse monoclonal RFP-Tag antibody for use in WB and ELISA in species independent samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | WB/ELISA |
| Host | Mouse |
| Reactivity | Species Independent |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Monoclonal |
| Clone ID | SMM5503 |
| Isotype | IgG1 |
| Conjugation | Unconjugated |
| Concentration | Lot specific |
| Purification | Affinity purification |
| Dilution Range | WB:1:5000-1:20000ELISA:Recommended starting concentration is 1 Mu g/mL. Please optimize the concentration based on your specific assay requirements. |
| Formulation | PBS with 0.02% Sodium Azide, 50% Glycerol, pH 7.3. |
Target Information
| Immunogen Sequence | MASSENVITEFMRFKVRMEG TVNGHEFEIEGEGEGRPYEG HNTVKLKVTKGGPLPFAWDI LSPQFQYGSKVYVKHPADIP DYKKLSFPEGFKWERVMNFE DGGVATVTQDSSLQDGCFIY KVKFIGVNFPSDGPVMQKKT MGWEASTERLYPRDGVLKGE THKALKLKDGGHYLVEFKSI YMAKKPVQLPGYYYVDAKLD ITSHNEDYTIVEQYERTEGR HHLFL |
| Specificity | Recombinant protein of RFP-Tag |
Additional Info
| Background | Protein tags are peptide sequences genetically grafted onto a recombinant protein. Often these tags are removable by chemical agents or by enzymatic means, such as proteolysis or intein splicing. Tags are attached to proteins for various purposes.Epitope tags are short peptide sequences which are chosen because high-affinity antibodies can be reliably produced in many different species. These are usually derived from viral genes, which explain their high immunoreactivity. Epitope tags include V5-tag, Myc-tag, HA-tag and NE-tag. These tags are particularly useful for western blotting, immunofluorescence and immunoprecipitation experiments, although they also find use in antibody purification. |
Information sourced from Uniprot.org