Product Details

Purity

>85% (SDS-PAGE)

Target Names

umuD

Uniprot No.

P0AG11

Alternative Names

umuD; b1183; JW1172Protein UmuD; EC 3.4.21.-; DNA polymerase V; Pol V) [Cleaved into: Protein UmuD']

Species

Escherichia coli (strain K12)

Expression Region

1-139

Target Protein Sequence

MLFIKPADLR EIVTFPLFSD LVQCGFPSPA ADYVEQRIDL NQLLIQHPSA TYFVKASGDS MIDGGISDGD LLIVDSAITA SHGDIVIAAV DGEFTVKKLQ LRPTVQLIPM NSAYSPITIS SEDTLDVFGV VIHVVKAMR

Protein Length

full length protein

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

Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp-complex may target Pol V to replication complexes stalled at DNA template lesions.

Gene References into Functions

There are multiple levels of regulation imposed on pol V including transcriptional control, posttranslational modification, targeted proteolysis, activation of the catalytic activity of pol V through protein-protein interactions and the very recently described intracellular spatial regulation of pol V. (Review) PMID: 27236212
The current study delves deeper into this process, initiating the task of mapping out the molecular details of the interaction between RecA and UmuD'2C PMID: 25811184
Like the self-cleaving serine proteases LexA and UmuD in Escherichia coli, UmuDAb required RecA for cleavage. PMID: 22697494
Electron paramagnetic resonance (EPR) spectroscopy study determined that the arms of UmuD2 display a large degree of motion, are largely unbound from the globular C-terminal domain, and that the free energy of dissociation is 2.1 kJ mol-1 PMID: 21975937
Study find that mutations of the N-terminal residues of loop 1, N32, N33, and D34, confer hypersensitivity to UV radiation and to 4-nitroquinoline-N-oxide and significantly reduce Pol V-dependent UV-induced mutagenesis. PMID: 21784925
Wild-type UmuD(2) and UmuD'(2) form exceptionally tight dimers in solution; however, we show that the single amino acid change N41D generates stable, active UmuD and UmuD' monomers that functionally mimic the dimeric wild-type proteins. PMID: 21118802
REVIEW: properties and functions of Pol V PMID: 15588845
In the absence of repair or when the repair capacity of the cell has been exceeded, translesion synthesis by polymerase V (Pol V) allows DNA synthesis to resume and is required to protect the arrested replication fork from degradation. PMID: 16199565
Lyase activity intrinsic to polymerase V PMID: 16202661
AlkB dioxygenase, PolV (UmuD'C), and AlkA have roles in preventing MMS-induced mutagenesis in Escherichia coli PMID: 16226494
found new class of UmuD variant proteins that fail to undergo cleavage but whose properties resemble those of the cleaved version, UmuD' PMID: 16464848
Structural characteristics of relatively poorly understood, intrinsically disordered umuD small dimeric proteins provide a model for the regulation of diverse aspects of the bacterial SOS response. PMID: 18216271

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Protein Families

Peptidase S24 family

Database Links

KEGG: ecj:JW1172

STRING: 511145.b1183

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Recombinant Escherichia coli Protein umuD (umuD)

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