AASS Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, FC, E |
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Primary Accession | Q9UDR5 |
Other Accession | NP_005754.2 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 102132 Da |
Antigen Region | 805-834 aa |
Gene ID | 10157 |
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Other Names | Alpha-aminoadipic semialdehyde synthase, mitochondrial, LKR/SDH, Lysine ketoglutarate reductase, LKR, LOR, Saccharopine dehydrogenase, SDH, AASS |
Target/Specificity | This AASS antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 805-834 amino acids from the C-terminal region of human AASS. |
Dilution | WB~~1:1000 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
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 | AASS Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | AASS (HGNC:17366) |
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Function | Bifunctional enzyme that catalyzes the first two steps in lysine degradation. |
Cellular Location | Mitochondrion. |
Tissue Location | Expressed in all 16 tissues examined with highest expression in the liver |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a bifunctional enzyme that catalyzes the first two steps in the mammalian lysine degradation pathway. The N-terminal and the C-terminal portions of this enzyme contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively, resulting in the conversion of lysine to alpha-aminoadipic semialdehyde. Mutations in this gene are associated with familial hyperlysinemia.
References
Sacksteder, K.A., et al. Am. J. Hum. Genet. 66(6):1736-1743(2000)
Papes, F., et al. Biochem. J. 344 PT 2, 555-563 (1999) :
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