Product Details

Purity

>85% (SDS-PAGE)

Target Names

UBI4

Uniprot No.

P0CG63

Alternative Names

UBI4; SCD2; YLL039C; Polyubiquitin [Cleaved into: Ubiquitin]

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Expression Region

1-76

Target Protein Sequence

MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG

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

Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.

Gene References into Functions

These results indicate that ubiquitination, a modification well known to target membrane proteins to the lysosome or vacuole for degradation, can also function as recycling signal to sort a SNARE into COPI vesicles in a non-degradative pathway. PMID: 29058666
ubi4 repeats modulate proteostasis and stress survival PMID: 28855501
Both Ssa1 and Ssa2 are essential for the ubiquitin-dependent degradation of short-lived proteins and the requirements of Ssa proteins and the co-chaperones widely vary depending on the conformations and folding status of the substrates. PMID: 27178214
Zap1 controls UBI4 by inducing transcription from an intragenic promoter, and the resulting truncated mRNA encodes only two of the five ubiquitin repeats. PMID: 27432887
study provided evidence that S65 phosphorylation of ubiquitin is a biologically important modification that influences nearly every step of the in vivo ubiquitin life cycle PMID: 26142280
Expression of UbQ2N-E64G in stress hypersensitive SUB60 cells decreased growth rate and prolonged half-life of substrates of UFD pathway, besides failure of complementation under heat and antibiotic stresses, so Gln2 and Glu64 have been conserved. PMID: 26548082
Ubiquitin signals proteolysis-independent stripping of transcription factors. PMID: 24613342
Data suggest that Ufd4 assembles the K29-linked ubiquitin chain(s) on Ub-P-betagal in vivo. PMID: 23726910
Data indicate that efficient formation of longer ubiquitin chains depends on the Cue1p CUE domain. PMID: 23665229
The expression a mutant human UBB analogous (UB14) in yeast markedly enhanced cellular susceptibility to toxic protein aggregates. PMID: 19214209

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Subcellular Location

Cytoplasm. Nucleus.

Protein Families

Ubiquitin family

Database Links

KEGG: sce:YLL039C

STRING: 4932.YLL039C

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Code	CSB-YP315569SVG
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP315569SVG
MSDS	MSDS
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Code	CSB-EP315569SVG-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-BP315569SVG
MSDS	MSDS
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Code	CSB-MP315569SVG
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Recombinant Saccharomyces cerevisiae Polyubiquitin (UBI4)

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