Reactivity | Hu, Mu, RtSpecies Glossary |
Applications | WB |
Clonality | Polyclonal |
Host | Sheep |
Conjugate | Unconjugated |
Concentration | LYOPH |
Immunogen | E. coli-derived recombinant human APBA2 Ala2-Leu165 Accession # Q99767 |
Specificity | Detects human APBA2 in direct ELISAs and human, mouse and rat in Western blots. In direct ELISAs, less than 1% cross-reactivity with recombinant human (rh) APBA1 and rhAPBA3 is observed. |
Source | N/A |
Isotype | IgG |
Clonality | Polyclonal |
Host | Sheep |
Gene | APBA2 |
Purity Statement | Antigen Affinity-purified |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Reconstitute at 0.2 mg/mL in sterile PBS. |
APBA2 (Adaptor protein X11 beta, also Mint2 and X11L) is a cytosolic member of the X11 family of adaptor proteins. Although its predicted MW is 83 kDa, it runs anomalously at 130-135 kDa in SDS-PAGE. APBA2 is expressed in neurons, and appears to play a role in A beta formation from APP. Normally, APBA2 associates with the cytoplasmic domain of transmembrane APP. This precludes its entry into lipid rafts, where it begins formation of A beta following cleaved by BACE. Human APBA2 is 749 amino acids (aa ) in length. It contains one phosphotyrosine binding (PTB) domain (aa 366-533) plus two PDZ domains (aa 568-734). Over aa 221-250, there is an APP interaction site that contains a key phosphorylation site at Ser238. There are two potential splice forms, one that shows a deletion of aa 406-417, and a second that contains a 44 aa substitution for aa 170-214. Over aa 1-165, human APBA2 shares 85% aa identity with mouse APBA2.
Secondary Antibodies |
Isotype Controls |
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