YMEL1 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 4
- PROTOCOLS
- BACKGROUND
Application ![]()
| FC, IHC-P, WB, E |
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Primary Accession | Q96TA2 |
Other Accession | Q925S8, O88967 |
Reactivity | Human, Hamster |
Predicted | Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 86455 Da |
Antigen Region | 191-219 aa |
Gene ID | 10730 |
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Other Names | ATP-dependent zinc metalloprotease YME1L1, 3424-, ATP-dependent metalloprotease FtsH1, Meg-4, Presenilin-associated metalloprotease, PAMP, YME1-like protein 1, YME1L1, FTSH1, YME1L |
Target/Specificity | This YMEL1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 191-219 amino acids from the N-terminal region of human YMEL1. |
Dilution | WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 |
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 | YMEL1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | YME1L1 |
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Synonyms | FTSH1, YME1L |
Function | ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:24315374, PubMed:26923599, PubMed:27786171, PubMed:31695197, PubMed:33237841, PubMed:36206740). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (PubMed:18076378, PubMed:26923599, PubMed:27495975, PubMed:33237841). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (PubMed:22262461). Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (PubMed:22262461). Involved in the mitochondrial adaptation in response to various signals, such as stress or developmental cues, by mediating degradation of mitochondrial proteins to rewire the mitochondrial proteome (PubMed:31695197). Catalyzes degradation of mitochondrial proteins, such as translocases, lipid transfer proteins and metabolic enzymes in response to nutrient starvation in order to limit mitochondrial biogenesis: mechanistically, YME1L is activated by decreased phosphatidylethanolamine levels caused by LPIN1 activity in response to mTORC1 inhibition (PubMed:31695197). Acts as a regulator of adult neural stem cell self-renewal by promoting mitochondrial proteome rewiring, preserving neural stem and progenitor cells self-renewal (By similarity). Required for normal, constitutive degradation of PRELID1 (PubMed:27495975). Catalyzes the degradation of OMA1 in response to membrane depolarization (PubMed:26923599). Mediates degradation of TIMM17A downstream of the integrated stress response (ISR) (PubMed:24315374). Catalyzes degradation of MICU1 when MICU1 is not assembled via an interchain disulfide (PubMed:36206740). |
Cellular Location | Mitochondrion inner membrane Mitochondrion |
Tissue Location | High expression in cardiac and skeletal muscle mitochondria. |

Provided below are standard protocols that you may find useful for product applications.
Background
YMEL1 is the human ortholog of yeast mitochondrial AAA metalloprotease, Yme1p. It is localized in the mitochondria and can functionally complement a yme1 disruptant yeast strain. It is proposed that this gene plays a role in mitochondrial protein metabolism and could be involved in mitochondrial pathologies.
References
Grupe, A., et al. Am. J. Hum. Genet. 78(1):78-88(2006)
Deloukas, P., et al. Nature 429(6990):375-381(2004)
Clark, H.F., et al. Genome Res. 13(10):2265-2270(2003)

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