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Mouse Anti-ALAD Recombinant Antibody (V2-180593) (CBMAB-A2129-YC)

Provided herein is a Mouse monoclonal antibody against Rat Aminolevulinate Dehydratase. The antibody can be used for immunoassay techniques, such as WB, ICC, IHC-P, IHC-Fr, ELISA.
See all ALAD antibodies

Summary

Host Animal
Mouse
Specificity
Rat
Clone
V2-180593
Antibody Isotype
IgG
Application
WB, ICC, IHC-P, C, ELISA

Basic Information

Immunogen
Aminolevulinate Delta Dehydratase
Host Species
Mouse
Specificity
Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB0.2-2 µg/ml
IF(ICC)5-20 µg/ml
IHC5-20 µg/ml

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Aminolevulinate Dehydratase
Introduction
The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin a
Entrez Gene ID
25374
UniProt ID
P06214
Alternative Names
Aminolevulinate Dehydratase; Porphobilinogen Synthase; Aminolevulinate, Delta-, Dehydratase; EC 4.2.1.24; ALADH; Delta-Aminolevulinic Acid Dehydratase; Testicular Tissue Protein Li 95; PBGS;
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.
Biological Process
Cellular response to interleukin-4 Source: Ensembl
Cellular response to lead ion Source: Ensembl
Heme biosynthetic process Source: UniProtKB
Negative regulation of proteasomal protein catabolic process Source: CAFA
Neutrophil degranulation Source: Reactome
Protein homooligomerization Source: UniProtKB
Protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Response to activity Source: Ensembl
Response to aluminum ion Source: Ensembl
Response to amino acid Source: Ensembl
Response to arsenic-containing substance Source: Ensembl
Response to cadmium ion Source: Ensembl
Response to cobalt ion Source: Ensembl
Response to drug Source: Ensembl
Response to ethanol Source: Ensembl
Response to fatty acid Source: Ensembl
Response to glucocorticoid Source: Ensembl
Response to herbicide Source: Ensembl
Response to hypoxia Source: Ensembl
Response to ionizing radiation Source: Ensembl
Response to iron ion Source: Ensembl
Response to lipopolysaccharide Source: Ensembl
Response to mercury ion Source: Ensembl
Response to methylmercury Source: Ensembl
Response to oxidative stress Source: Ensembl
Response to platinum ion Source: Ensembl
Response to selenium ion Source: Ensembl
Response to vitamin B1 Source: Ensembl
Response to vitamin E Source: Ensembl
Response to zinc ion Source: Ensembl
Cellular Location
Cytosol; Extracellular exosome; Extracellular region; Nucleus; Ficolin-1-rich granule lumen; Secretory granule lumen
Involvement in disease
Acute hepatic porphyria (AHEPP): A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralyses and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors.

Yohannes, Y. B., Nakayama, S. M., Yabe, J., Toyomaki, H., Kataba, A., Nakata, H., ... & Ishizuka, M. (2021). Delta-aminolevulinic acid dehydratase (ALAD) and vitamin D receptor (VDR) genes polymorphisms in children residing in an abandoned lead‑zinc mine area in Kabwe, Zambia. Meta Gene, 27, 100838.

Bah, H. A., Dos Anjos, A. L. S., Gomes-Júnior, E. A., Bandeira, M. J., de Carvalho, C. F., Dos Santos, N. R., ... & Menezes-Filho, J. A. (2021). Delta-Aminolevulinic Acid Dehydratase, Low Blood Lead Levels, Social Factors, and Intellectual Function in an Afro-Brazilian Children Community. Biological Trace Element Research, 1-11.

Hamid, O. I. A., Khayal, E. E. S. H., Tolba, S. A. R., & Orabi, E. E. (2020). Maternal Δ-aminolevulinic acid dehydratase 1-2 genotype enhances fetal lead exposure and increases the susceptibility to the development of cerebral palsy. Environmental Science and Pollution Research, 27(36), 44709-44723.

Saliu, J. A., Ademiluyi, A. O., Boligon, A. A., Oboh, G., Schetinger, M. R. C., & Rocha, J. B. T. (2019). Dietary supplementation of jute leaf (Corchorus olitorius) modulates hepatic delta‐aminolevulinic acid dehydratase (δ‐ALAD) activity and oxidative status in high‐fat fed/low streptozotocin‐induced diabetic rats. Journal of food biochemistry, 43(8), e12949.

Neeleman, R. A., van Beers, E. J., Friesema, E. C., Koole‐Lesuis, R., van der Pol, W. L., Wilson, J. P., & Langendonk, J. G. (2019). Clinical Remission of Delta‐Aminolevulinic Acid Dehydratase Deficiency Through Suppression of Erythroid Heme Synthesis. Hepatology (Baltimore, Md.), 70(1), 434.

Mani, M. S., Kunnathully, V., Rao, C., Kabekkodu, S. P., Joshi, M. B., & D’Souza, H. S. (2018). Modifying effects of δ-Aminolevulinate dehydratase polymorphism on blood lead levels and ALAD activity. Toxicology letters, 295, 351-356.

Ge, J., Yu, Y., Xin, F., Yang, Z. J., Zhao, H. M., Wang, X., ... & Cao, X. C. (2017). Downregulation of delta‐aminolevulinate dehydratase is associated with poor prognosis in patients with breast cancer. Cancer science, 108(4), 604-611.

La-Llave-León, O., Méndez-Hernández, E. M., Castellanos-Juárez, F. X., Esquivel-Rodríguez, E., Vázquez-Alaniz, F., Sandoval-Carrillo, A., ... & Salas-Pacheco, J. M. (2017). Association between blood lead levels and delta-aminolevulinic acid dehydratase in pregnant women. International journal of environmental research and public health, 14(4), 432.

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For research use only. Not intended for any clinical use.

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