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Mouse Anti-ALAS1 Recombinant Antibody (V2-634205) (CBMAB-AP249LY)


See all ALAS1 antibodies
Published Data
Mouse Anti-ALAS1 Recombinant Antibody (CAP102) in WB
Mitochondrial protein analysis by Western blot. ...View More
Bruhn, C., Bastianello, G., & Foiani, M. (2022). Cancer cell histone density links global histone acetylation, mitochondrial proteome and histone acetylase inhibitor sensitivity. Communications Biology, 5(1), 882.
Mouse Anti-ALAS1 Recombinant Antibody (CAP102) in WB
FECH knockdown resulted in the accumulation of PpIX. (A) Western blot images showing the level of heme biosynthesis enzymes in vector control and FECH-knockdown SkBr3 cells. (B, C) The band intensity of ALAS-H (B) and FECH (C) was quantified and shown (n=3). Bars represent the standard deviation (SD). ** P < 0.01, *** P < 0.001, compared with vector control. (D, E) Fluorescence emission spectra of PpIX standard (125 ng/mL) and cell lysates without (D) or with (E) ALA (1 mM for 4 h). All fluorescence spectra were measured using 400 ± 2.5 nm excitation. ...View More
Palasuberniam, P., Kraus, D., Mansi, M., Braun, A., Howley, R., Myers, K. A., & Chen, B. (2019). Ferrochelatase deficiency abrogated the enhancement of aminolevulinic acid-mediated protoporphyrin IX by iron chelator deferoxamine. Photochemistry and photobiology, 95(4), 1052-1059.

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-634205
Antibody Isotype
IgG1, κ
Application
ICC, IF, WB, IP , ELISA

Basic Information

Immunogen
Amino acids 57-210 mapping near the N-terminus of ALAS-H of human origin.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
ELISA1:30-1:3,000
IF(ICC)1:50-1:500

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
5'-Aminolevulinate Synthase 1
Introduction
This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. The enzyme encoded by this gene is the housekeeping enzyme; a separate gene encodes a form of the enzyme that is specific for erythroid tissue. The level of the mature encoded protein is regulated by heme: high levels of heme down-regulate the mature enzyme in mitochondria while low heme levels up-regulate. A pseudogene of this gene is located on chromosome 12. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jan 2015]
Entrez Gene ID
211
UniProt ID
P13196
Alternative Names
5'-Aminolevulinate Synthase 1; 5-Aminolevulinate Synthase 1; Aminolevulinate, Delta-, Synthase 1; Delta-Aminolevulinate Synthase 1; 5-Aminolevulinic Acid Synthase 1; Delta-ALA Synthase 1; EC 2.3.1.37; ALAS-H;
Biological Process
Erythrocyte development Source: GO_Central
Heme biosynthetic process Source: GO_Central
Hemoglobin biosynthetic process Source: GO_Central
Mitochondrion organization Source: Reactome
Protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Regulation of metabolic process Source: Reactome
Response to hypoxia Source: GO_Central
Cellular Location
Mitochondrion matrix

Lahiji, A. P., Anderson, K. E., Chan, A., Simon, A., Desnick, R. J., & Ramanujam, V. S. (2020). 5-Aminolevulinate dehydratase porphyria: Update on hepatic 5-aminolevulinic acid synthase induction and long-term response to hemin. Molecular Genetics and Metabolism, 131(4), 418-423.

Stojanovski, B. M., Hunter, G. A., Na, I., Uversky, V. N., Jiang, R. H., & Ferreira, G. C. (2019). 5-Aminolevulinate synthase catalysis: the catcher in heme biosynthesis. Molecular genetics and metabolism, 128(3), 178-189.

Badawy, A. A. B. (2019). Hypothesis: Metabolic targeting of 5-aminolevulinate synthase by tryptophan and inhibitors of heme utilisation by tryptophan 2, 3-dioxygenase as potential therapies of acute hepatic porphyrias. Medical hypotheses, 131, 109314.

Na, I., Catena, D., Kong, M. J., Ferreira, G. C., & Uversky, V. N. (2018). Anti-correlation between the dynamics of the active site loop and C-terminal tail in relation to the homodimer asymmetry of the mouse erythroid 5-aminolevulinate synthase. International journal of molecular sciences, 19(7), 1899.

Ikushiro, H., Nagami, A., Takai, T., Sawai, T., Shimeno, Y., Hori, H., ... & Yano, T. (2018). Heme-dependent inactivation of 5-aminolevulinate synthase from Caulobacter crescentus. Scientific reports, 8(1), 1-13.

Na, I., DeForte, S., Stojanovski, B. M., Ferreira, G. C., & Uversky, V. N. (2018). Molecular dynamics analysis of the structural and dynamic properties of the functionally enhanced hepta-variant of mouse 5-aminolevulinate synthase. Journal of Biomolecular Structure and Dynamics, 36(1), 152-165.

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

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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