Recombinant Human UPD protein is a Human Full Length protein, in the 1 to 367 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, MS
No
M G S S H H H H H H S S G L V P R G S H M E A N G L G P Q G F P E L K N D T F L R A A W G E E T D Y T P V W C M R Q A G R Y L P E F R E T R A A Q D F F S T C R S P E A C C E L T L Q P L R R F P L D A A I I F S D I L V V P Q A L G M E V T M V P G K G P S F P E P L R E E Q D L E R L R D P E V V A S E L G Y V F Q A I T L T R Q R L A G R V P L I G F A G A P W T L M T Y M V E G G G S S T M A Q A K R W L Y Q R P Q A S H Q L L R I L T D A L V P Y L V G Q V V A G A Q A L Q L F E S H A G H L G P Q L F N K F A L P Y I R D V A K Q V K A R L R E A G L A P V P M I I F A K D G H F A L E E L A Q A G Y E V V G L D W T V A P K K A R E C V G K T V T L Q V N L D P C A L Y A S E E E I G Q L V K Q M L D D F G P H R Y I A N L G H G L Y P D M D P E H V G A F V D A V H K H S R L L R Q N
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
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).
Uroporphyrinogen decarboxylase, UPD, URO-D, UROD
Recombinant Human UPD protein is a Human Full Length protein, in the 1 to 367 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, MS
No
No
Human
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
M G S S H H H H H H S S G L V P R G S H M E A N G L G P Q G F P E L K N D T F L R A A W G E E T D Y T P V W C M R Q A G R Y L P E F R E T R A A Q D F F S T C R S P E A C C E L T L Q P L R R F P L D A A I I F S D I L V V P Q A L G M E V T M V P G K G P S F P E P L R E E Q D L E R L R D P E V V A S E L G Y V F Q A I T L T R Q R L A G R V P L I G F A G A P W T L M T Y M V E G G G S S T M A Q A K R W L Y Q R P Q A S H Q L L R I L T D A L V P Y L V G Q V V A G A Q A L Q L F E S H A G H L G P Q L F N K F A L P Y I R D V A K Q V K A R L R E A G L A P V P M I I F A K D G H F A L E E L A Q A G Y E V V G L D W T V A P K K A R E C V G K T V T L Q V N L D P C A L Y A S E E E I G Q L V K Q M L D D F G P H R Y I A N L G H G L Y P D M D P E H V G A F V D A V H K H S R L L R Q N
Full Length
43 kDa
1 to 367
Recombinant
His tag N-Terminus
Liquid
ab96770 is purified using conventional chromatography techniques.
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).
Belongs to the uroporphyrinogen decarboxylase family.
Blue Ice
-20°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
Previously labelled as UROD.
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.
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.
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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15% SDS-PAGE showing ab96770 at approximately 43.0kDa (3µg).
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