JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB124318

Recombinant Human ALAD protein (His tag N-Terminus)

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant Human ALAD protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 330 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Delta-aminolevulinic acid dehydratase, ALADH, Porphobilinogen synthase, ALAD

1 Images
SDS-PAGE - Recombinant Human ALAD protein (His tag N-Terminus) (AB124318)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human ALAD protein (His tag N-Terminus) (AB124318)

ab124318 at 3 μg analysed by 15% SDS-PAGE.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P13716

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl

storage-buffer

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>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSHMQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE","proteinLength":"Full Length","predictedMolecularWeight":"38.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":330,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P13716","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The ALAD also known as Aminolevulinate Dehydratase is an essential enzyme involved in the biosynthesis of heme facilitating the condensation of two molecules of aminolevulinic acid to form porphobilinogen. The enzyme has a molecular mass of approximately 36 kDa. It is ubiquitously expressed across various tissues with notable activity in the liver and erythroid precursor cells within the bone marrow where heme biosynthesis is essential for the production of hemoglobin.
Biological function summary

The enzyme plays an important role in the early steps of the heme biosynthetic pathway. ALAD forms part of a multi-step process critical for heme production which is an important component of hemoglobin myoglobin and various cytochromes. The enzyme operates as a metalloenzyme requiring zinc for its activity and is subject to regulation by metal ion availability and substrate concentrations. Alterations in its activity can have significant impacts on cellular iron utilization and red blood cell function.

Pathways

ALAD plays a critical role within the heme biosynthesis pathway linking amino acid metabolism to porphyrin and heme production. It connects tightly with other enzymes involved in this pathway such as porphobilinogen deaminase. ALAD's function ensures the steady supply of intermediates necessary for synthesizing heme which serves further purposes in electron transport and oxygen transport systems within cells.

The improper function of ALAD associates with conditions such as lead poisoning and acute intermittent porphyria. In lead poisoning lead ions inhibit ALAD activity resulting in the accumulation of its substrate aminolevulinic acid and subsequent disturbances in heme production. In acute intermittent porphyria mutations in ALAD or interacting proteins like porphobilinogen deaminase can influence enzyme efficiency and increase the risk of metabolic crises. Understanding ALAD's role offers potential therapeutic insights for managing these disorders.

Specifications

Form

Liquid

Additional notes

ab124318 was purified by using conventional chromatography techniques.

General info

Function

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.

Sequence similarities

Belongs to the ALAD family.

Product protocols

Target data

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
See full target information ALAD

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com