Product Details

Purity

>85% (SDS-PAGE)

Target Names

ftsH

Uniprot No.

P0AAI3

Alternative Names

ftsH; hflB; mrsC; std; tolZ; b3178; JW3145ATP-dependent zinc metalloprotease FtsH; EC 3.4.24.-; Cell division protease FtsH

Species

Escherichia coli (strain K12)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

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.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

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.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

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

Datasheet

Please contact us to get it.

Target Background

Function

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.; As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS).; (Microbial infection) Probably transports the toxic C-terminal region of CdiA from E.coli strain 536, E.cloacae strain ATCC 13047 and of Y.pestis strain A across the inner membrane to the cytoplasm, where CdiA has a toxic effect. Toxin transport is strain-specific, mutations in this gene do not confer resistance to several other tested CdiA toxins.

Gene References into Functions

FtsH-mediated coordination of lipopolysaccharide biosynthesis correlates with the growth rate. PMID: 23417489
FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm. PMID: 21700705
report the first purification of E. coli HflK and HflC separately as active and functional proteins and show that each can interact with HflB on its own and each inhibits the proteolysis of lambdaCII PMID: 20599668
show that FtsH exists exclusively as a large complex, termed FtsH holo-enzyme, which can be separated from bulk of membrane proteins after detergent solubilization and velocity sedimentation; a tentative model is presented PMID: 15037243
FtsH hexamer degrades approximately 0.5 molecules of Cy3-sigma32 per min at 42 degrees C and hydrolyzes approximately 140 ATP molecules during the degradation of a single molecule of Cy3-sigma32 PMID: 15037246
The in vivo stability of the mutated RpoH proteins correlated with their stability in a purified in vitro degradation system, suggesting that region 2.1 might be directly involved in the interaction with the FtsH protease. PMID: 17660420
The mechanism of lambda CIII inhibition of E. coli HflB was studied. PMID: 17890311
inhibition of HflB-mediated proteolysis of sigma(32) by CIII is very similar to that of lambdaCII, characterized by an enhanced protection by the core CIII peptide CIIIC (amino acids 14-41 of lambdaCIII) & lack of interaction between sigma(32) & CIII. PMID: 18721134
Data show that FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of LPS. PMID: 18776015
RpoH fragment composed of residues 37-147 is degraded in an FtsH-dependent manner. PMID: 19025566

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Subcellular Location

Cell inner membrane; Multi-pass membrane protein.

Protein Families

AAA ATPase family; Peptidase M41 family

Database Links

KEGG: ecj:JW3145

STRING: 316385.ECDH10B_3352

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Code	CSB-EP359465ENV-B
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Code	CSB-MP359465ENV
MSDS	MSDS
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Recombinant Escherichia coli ATP-dependent zinc metalloprotease FtsH (ftsH), partial

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