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Recombinant Human UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), partial

Recombinant Human UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), partial

Code	CSB-YP878928HU
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP878928HU
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP878928HU-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP878928HU
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP878928HU
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

UGGT1

Uniprot No.

Q9NYU2

Alternative Names

GT; HUGT1; UDP glucose glycoprotein glucosyltransferase 1; UDP Glucose Glycoprotein Glucosyltransferase; UDP--Glc:glycoprotein glucosyltransferase; UDP-glucose ceramide glucosyltransferase-like 1; UDP-glucose:glycoprotein glucosyltransferase 1; UGCGL1; UGGG1; UGGG1_HUMAN; UGGT; Uggt1; UGT1; UGTR

Species

Homo sapiens (Human)

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.

Customer Reviews and Q&A

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Target Background

Function

Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation.

Gene References into Functions

both vIL-6 and VKORC1v2 interact with calnexin cycle proteins UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), which catalyzes monoglucosylation of N-glycans, and oppositely acting glucosidase II (GlucII), and that vIL-6 can promote protein folding. PMID: 28878084
These findings provide important insight on the role of unfolded protein response (UPR) and host UGGT1 in regulating RNA virus replication and pathogenicity. PMID: 28545059
The results demonstrated that FAM5C is an N-glycosylated protein, and N-glycosylation by UGGT1 is necessary for the secretion of FAM5C. PMID: 28351617
A novel UGGT1- and p97-dependent protein quality checkpoint is shown. This checkpoint is alerted to prevent secretion of a polypeptide that passes the luminal quality control scrutiny by BiP and CNX but contains an intramembrane ionizable residue. PMID: 25694454
Kyte-Doolittle analysis as well as homology modeling revealed a cluster of hydrophobic amino acids that may be functional in the folding sensing mechanism of HUGT1 PMID: 26196150
Results indicate that glycan structures are similar to endogenous glycans at low expression levels of uridine 5'-diphosphate-glucose: glycoprotein glucosyltransferase (UGGT1). PMID: 25935482
The UGGT1 is a well-documented enzyme which functions as a folding sensor in the endoplasmic reticulum, by the virtue of its ability to transfer a glucose residue to non-glucosylated high-mannose-type glycans of immature glycoproteins. PMID: 24415556
UGT1 aids in the folding of sequential domain-containing proteins such as prosaposin. PMID: 20498017
The substrate binding specificity PMID: 12682060
the amino-terminal 80% of HUGT1 is required for activation of the catalytic domain PMID: 12913004
overexpression leads to increase in production of recombinant proteins; gene targeting PMID: 19466607