R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
BCL2L13 (E6G1Q) Rabbit mAb #61974
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 90 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
BCL2L13 (E6G1Q) Rabbit mAb recognizes endogenous levels of total BCL2L13 protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu267 of human BCL2L13 protein.
Background
BCL2L13 (Bcl-2-like protein 13, Bcl-rambo) is an atypical member of the Bcl-2 family of proteins that regulate apoptosis at the mitochondria (1). While it contains conserved Bcl-2 homology (BH) domains -1, -2, -3, and -4, it has a unique C-terminal region and does not interact with other Bcl-2 family members (1). BCL2L13 may regulate apoptosis in a cellular context manner (reviewed in 2). It was originally identified as a pro-apoptotic protein with activity dependent on its C-terminal region (1). Interaction with the adenine nucleotide translocator (ANT) suppresses the ADP/ATP-dependent translocation activity of ANT (3). Other studies have found that BCL2L13 can inhibit apoptosis in glioblastoma and tumor growth (4). These studies found that BCL2L13 binds to pro-apoptotic ceramide synthases 2 (CerS2) and 6 (CerS6) and blocks homo- and heteromeric CerS2/6 complex formation and activity. Studies have also found that BCL2L13 can regulate mitochondrial fragmentation and can bind to LC3 to facilitate the clearance of damaged mitochondria through mitophagy (5,6).
- Kataoka, T. et al. (2001) J Biol Chem 276, 19548-54.
- Kataoka, T. (2022) Front Cell Dev Biol 10, 1065702.
- Kim, J.Y. et al. (2012) FEBS Lett 586, 3142-9.
- Jensen, S.A. et al. (2014) Proc Natl Acad Sci USA 111, 5682-7.
- Murakawa, T. et al. (2015) Nat Commun 6, 7527.
- Otsu, K. et al. (2015) Autophagy 11, 1932-3.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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