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AB79941

Recombinant Human ALAS2/ASB protein (His tag N-Terminus)

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Recombinant Human ALAS2/ASB protein (His tag N-Terminus) is a Human Fragment protein, in the 136 to 553 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

ALASE, ASB, ALAS2, ALAS-E, 5-aminolevulinic acid synthase 2, Delta-ALA synthase 2, Delta-aminolevulinate synthase 2

1 Images
SDS-PAGE - Recombinant Human ALAS2/ASB protein (His tag N-Terminus) (AB79941)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human ALAS2/ASB protein (His tag N-Terminus) (AB79941)

105 SDS-PAGE showing ab79941 at approximately 46kDa (8μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P22557

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00053% PLP

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>" } } }
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Product details

This product was previously labelled as ALAS2
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Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":553,"aminoAcidStart":136,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P22557","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°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.

ALAS2 also known as 5-aminolevulinate synthase 2 is an important enzyme in heme biosynthesis. This enzyme is specific to erythroid cells and it catalyzes the first step in the formation of heme. ALAS2 has an approximate molecular weight of 65 kDa and it is mainly expressed in the mitochondria of erythroblasts in the bone marrow. It functions mechanistically by directing the condensation of glycine and succinyl-CoA to form delta-aminolevulinic acid (ALA) which is important for subsequent steps in heme production.
Biological function summary

ALAS2 plays a significant role in erythropoiesis as it contributes to heme production which is necessary for hemoglobin assembly. ALAS2 is not known to be part of a complex per se but its function is regulated allosterically by iron availability and activity levels. The synthesis of heme is required for proper formation of red blood cells and ALAS2's regulatory mechanisms ensure that heme is synthesized in synchrony with iron levels.

Pathways

ALAS2 acts as an initiator of the heme biosynthesis pathway which connects to the larger porphyrin metabolism pathway. This pathway involves additional proteins such as ferrochelatase and uroporphyrinogen III synthase. ALAS2's activity influences the overall efficiency of heme production and in turn iron metabolism. The regulation of ALAS2 by iron levels is a quintessential example of the coordination between cellular metabolism and iron availability in the erythroid lineage.

ALAS2 mutations associate with X-linked sideroblastic anemia a condition characterized by defective heme synthesis in erythroid cells. Relatedly heme biosynthesis dysregulation links to conditions like porphyria. In X-linked sideroblastic anemia malfunction of ALAS2 affects the activity of other enzymes involved in the heme production pathway leading to iron accumulation in mitochondria and ineffective erythropoiesis. Researchers also find connections between ALAS2 and proteins like ferrochelatase in the context of these disorders further impacting the understanding of heme-related diseases.
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Specifications

Form

Liquid

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General info

Function

Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed : 14643893, PubMed : 21252495, PubMed : 21309041, PubMed : 21653323, PubMed : 32499479, PubMed : 34492704). Contributes significantly to heme formation during erythropoiesis (PubMed : 2050125).. Isoform 3. Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed : 14643893). Catalytic activity is 75-85% of isoform 1 activity (PubMed : 14643893).. Isoform 4. Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed : 14643893). Catalytic activity is 65-75% of isoform 1 activity (PubMed : 14643893).

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Subcellular localisation

Mitochondrion matrix

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Product protocols

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Target data

Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed : 14643893, PubMed : 21252495, PubMed : 21309041, PubMed : 21653323, PubMed : 32499479, PubMed : 34492704). Contributes significantly to heme formation during erythropoiesis (PubMed : 2050125).. Isoform 3. Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed : 14643893). Catalytic activity is 75-85% of isoform 1 activity (PubMed : 14643893).. Isoform 4. Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed : 14643893). Catalytic activity is 65-75% of isoform 1 activity (PubMed : 14643893).
See full target information ALAS2
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