ABAD Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
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Primary Accession | Q6IBS9 |
Other Accession | O70351, O08756, Q99714, O02691 |
Reactivity | Human, Mouse |
Predicted | Bovine, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Antigen Region | 199-235 aa |
Other Names | hydroxyacyl-Coenzyme A dehydrogenase, type II isoform 1; 3-hydroxyacyl-CoA dehydrogenase type II; Type II HADH; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; Endoplasmic reticulum-associated amyloid beta-peptide binding protein; Short-chain type dehydrogenase/reductase XH98G2 ; ERAB, HSD17B10, SCHAD; HADH2 protein |
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Target/Specificity | This ABAD antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 199-235 amino acids from the C-terminal region of human ABAD. |
Dilution | WB~~1:1000 IHC-P~~1:50~100 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | ABAD Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Amyloid b-peptide-binding alcohol dehydrogenase (ABAD) is a member of the family of short chain dehydrogenase/reductases; unique among this family, it binds amyloid b-peptide and exhibits enzymatic activity toward a wide variety of substrates including linear alcohols. In an amyloid beta-abundant environment, ABAD appears to trigger cell stress induced by the amyloid peptide.
References
FASEB J. 19 (6), 597-598 (2005) J. Mol. Biol. 342 (3), 943-952 (2004) Science 304 (5669), 448-452 (2004) FEBS Lett. 451 (3), 238-242 (1999) J. Biol. Chem. 274 (21), 15014-15019 (1999)
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