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LIPT2 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | A6NK58 |
| Other Accession | NP_001138341.1 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 25195 Da |
| Antigen Region | 13-43 aa |
| Gene ID | 387787 |
|---|---|
| Other Names | Putative lipoyltransferase 2, mitochondrial, Lipoate-protein ligase B, Lipoyl/octanoyl transferase, Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase, LIPT2 |
| Target/Specificity | This LIPT2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 13-43 amino acids from the N-terminal region of human LIPT2. |
| Dilution | WB~~1:1000 |
| 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 | LIPT2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | LIPT2 (HGNC:37216) |
|---|---|
| Function | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein (octanoyl-ACP) onto the lipoyl domains of lipoate-dependent enzymes such as the protein H of the glycine cleavage system (GCSH) (PubMed:28757203). Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). |
| Cellular Location | Mitochondrion |
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Provided below are standard protocols that you may find useful for product applications.
Background
LIPT2 catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
References
Venter, J.C., et al. Science 291(5507):1304-1351(2001)
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