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AB96770

Recombinant Human UPD protein

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Recombinant Human UPD protein is a Human Full Length protein, in the 1 to 367 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Uroporphyrinogen decarboxylase, UPD, URO-D, UROD

1 Images
SDS-PAGE - Recombinant Human UPD protein (AB96770)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human UPD protein (AB96770)

15% SDS-PAGE showing ab96770 at approximately 43.0kDa (3µg).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

P06132

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0292% EDTA, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Previously labelled as UROD.
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQVNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN","proteinLength":"Full Length","predictedMolecularWeight":"43 kDa","actualMolecularWeight":null,"aminoAcidEnd":367,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P06132","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The ubiquitously expressed UDP-glucuronosyltransferase protein family often referred to as UGTs plays essential roles in the detoxification and metabolism of both endogenous and exogenous compounds. Individual UGT enzymes convert lipophilic molecules into more water-soluble glucuronides facilitating their excretion. This process involves the transfer of glucuronic acid from uridine diphosphate glucuronic acid (UDPGA) to substrates. UGTs display diverse tissue expression with significant activity in the liver gastrointestinal tract and kidneys. These enzymes typically have a molecular mass of around 50-60 kDa.
Biological function summary

UDP-glucuronosyltransferases are integral to phase II metabolism transforming small hydrophobic molecules for elimination. The UGT family functions within the microsomal enzyme system and associates with lipid membranes in the endoplasmic reticulum. UGTs work as monomers or form enzyme complexes particularly with other phase II enzymes such as sulfotransferases to efficiently manage the body's biochemical landscape. They recognize a wide range of substrates including hormones bile acids and drugs highlighting their metabolic versatility.

Pathways

UDP-glucuronosyltransferases participate primarily in the detoxification pathway. This pathway relies on UGTs for the conjugation of xenobiotics aiding in detoxifying harmful compounds. The enzymes also integrate into the bilirubin metabolic pathway where they catalyze the conjugation of bilirubin reducing its toxicity. Notably UGT1A1 a member of the UGT family takes part in this pathway and interacts with other proteins such as cytochrome P450 enzymes which are important in drug metabolism and synthesis of cholesterol steroids and other lipids.

Defects or deficiencies in UDP-glucuronosyltransferases can lead to clinical conditions like Gilbert's syndrome and Crigler-Najjar syndrome. Gilbert's syndrome results from mutations in UGT1A1 causing mild unconjugated hyperbilirubinemia. Crigler-Najjar syndrome a more severe disorder arises from significantly impaired UGT1A1 function leading to extreme cases of hyperbilirubinemia that may require liver transplantation. The interrelationship between UGT1A1 and proteins like albumin which binds bilirubin in the bloodstream highlights the important impact of glucuronidation in maintaining bilirubin homeostasis.
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Specifications

Form

Liquid

Additional notes

ab96770 is purified using conventional chromatography techniques.

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General info

Function

Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway (PubMed : 11069625, PubMed : 11719352, PubMed : 14633982, PubMed : 18004775, PubMed : 21668429). Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme (PubMed : 11069625, PubMed : 11719352, PubMed : 14633982, PubMed : 21668429). In vitro also decarboxylates pentacarboxylate porphyrinogen I (PubMed : 12071824).

Sequence similarities

Belongs to the uroporphyrinogen decarboxylase family.

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Product protocols

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Target data

Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway (PubMed : 11069625, PubMed : 11719352, PubMed : 14633982, PubMed : 18004775, PubMed : 21668429). Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme (PubMed : 11069625, PubMed : 11719352, PubMed : 14633982, PubMed : 21668429). In vitro also decarboxylates pentacarboxylate porphyrinogen I (PubMed : 12071824).
See full target information UROD
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