Anti-ATTR/Transthyretin amyloidosis antibody [NI301A] (STJA0021585)
SPECIFICATIONS
ClonalityMonoclonal
HostMouse
ConjugationUnconjugated
IsotypeIgG2a
General Information
| Short Description | Mouse monoclonal Transthyretin antibody for use in ELISA, IHC, IF, Neut, SPR and WB in samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | ELISA/IHC/IF/Neut/SPR/WB |
| Host | Mouse |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO) MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS |
Product Properties
| Clonality | Monoclonal |
| Clone ID | NI301A |
| Isotype | IgG2a |
| Conjugation | Unconjugated |
| Concentration | 0.75 mg/mL |
| Purification | Protein A/G purified from cell culture supernatant |
| Formulation | 0.01M PBS, pH 7.4. |
| Storage Instruction | Suitable for storage at +4°C between 1-2 weeks For longer term store at-20°C for up to 12 months |
Target Information
| Gene Symbol | TTR |
| Gene ID | 7276 |
| Uniprot ID | TTHY_HUMAN |
Additional Info
| Post Translational Modifications | Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYLD1 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway. Sulfonation of the reactive cysteine Cys-30 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation. |
| Function | Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. |
| Protein Name | TransthyretinAttrPrealbuminTbpa |
| Database Links | Reactome: R-HSA-2453902Reactome: R-HSA-3000171Reactome: R-HSA-6798695Reactome: R-HSA-975634Reactome: R-HSA-977225Reactome: R-HSA-9918449 |
| Cellular Localisation | SecretedCytoplasm |
| Alternative Antibody Names | Anti-Transthyretin antibodyAnti-Attr antibodyAnti-Prealbumin antibodyAnti-Tbpa antibodyAnti-TTR antibodyAnti-PALB antibody |
Information sourced from Uniprot.org