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Recombinant Human ATP-dependent zinc metalloprotease YME1L1 (YME1L1), partial

Recombinant Human ATP-dependent zinc metalloprotease YME1L1 (YME1L1), partial

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Target Background

Product Details

Abbreviation

YME1L1

Purity

>85% (SDS-PAGE)

Target Names

YME1L1

Uniprot NO.

Q96TA2

Alternative Names

YME1L1; FTSH1; YME1L; UNQ1868/PRO4304; ATP-dependent zinc metalloprotease YME1L1; ATP-dependent metalloprotease FtsH1; Meg-4; Presenilin-associated metalloprotease; PAMP; YME1-like protein 1

Species

Homo sapiens (Human)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region. 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. 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. Required for normal, constitutive degradation of PRELID1. Catalyzes the degradation of OMA1 in response to membrane depolarization. Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1).

Gene References into Functions

Data show that engineered YME1L protease discriminates between degradation signals by amino acid composition, implying the use of sequence-specific signals in mitochondrial proteostasis. PMID:27786171
These results identify mutations in YME1L1 as a cause of a mitochondriopathy with optic nerve atrophy highlighting the importance of YME1L1 for mitochondrial functionality in humans. PMID:27495975
YME1L1 was identified as the first NUMT (nuclear mtDNA) suppressor gene in human and demonstrate that inactivation of YME1L1 induces migration of mtDNA to the nuclear genome. PMID:28356157
differential stress-induced degradation of YME1L and OMA1 as a mechanism for sensitively adapting mitochondrial inner membrane protease activity and function in response to distinct types of cellular insults. PMID:26923599
YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress.Loss of YME1L compromises the regulation of mitochondrial inner membrane proteostasis. PMID:25433032
Results reveal a crucial role for YME1L in the maintenance of mitochondrial inner-membrane proteostasis and in the proteolytic regulation of respiratory chain biogenesis. PMID:22262461