Monoclonal Anti-Seladin-1 antibody produced in mouse

~2 mg/mL, clone SL-14, purified immunoglobulin, buffered aqueous solution

Anti-Selective Alzheimer’s disease indicator-1, Anti-24-dehydro-cholesterol reductase (DCHR24), Anti-Diminuto/Dwarf-1 homolog
MDL number:

Quality Level

biological source


antibody form

purified immunoglobulin

antibody product type

primary antibodies


SL-14, monoclonal


buffered aqueous solution

mol wt

antigen ~60 kDa

species reactivity



antibody small pack of 25 μL


~2 mg/mL


immunocytochemistry: suitable
indirect ELISA: suitable
western blot: 1-2 μg/mL using extracts of HEK-293T cells expressing human seladin-1





UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

human ... DHCR24(1718)

General description

Monoclonal Anti-Seladin-1 (mouse IgG2b isotype) is derived from the hybridoma SL-14 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to human seladin-1.Seladin-1 is a human homolog of the Diminuto/Dwarf1 gene described in plants and C elegans. Seladin-1 (selective alzheimer′s disease indicator-1, 60 kDa) is encoded by the DHCR24 (3-β-hydroxysterol-Δ-24- reductase) gene. Seladin-1 is mainly located in the endoplasmic reticulum.


synthetic peptide corresponding to amino acids 505-516 of human seladin-1, conjugated to KLH.


Monoclonal Anti-Seladin-1 antibody produced in mouse has been used in:
  • enzyme linked immunosorbent assay (ELISA),
  • immunoblotting
  • immunocytochemistry

Biochem/physiol Actions

Seladin-1 (selective Alzheimer′s disease indicator-1, 60 kDa), is an anti-apoptotic protein, found to be down regulated in large pyramidal neurons in brain regions affected by Alzheimer′s disease (AD). It is a flavin-adenine-dinucleotide (FAD)-dependent oxidoreductase, involved in cholesterol homeostasis. It catalyzes the conversion of desmosterol to cholesterol. It prevents apoptosis via inhibition of caspase-3, a key mediator of the apoptotic cascade, suggesting that seladin-1 may be involved in the regulation of cell survival and death. Seladin-1 has been shown to function as a key mediator of Ras-induced senescence in mouse and human fibroblasts. In response to oncogenic and oxidative stress, seladin-1 binds to p53 and displaces the E3 ubiquitin ligase Mdm2 from p53, resulting in accumulation of p53. The expression of seladin-1 has been reported to be up-regulated in adrenocortical adenomas and in some tumors.

Physical form

Solution in 0.01 M phophate buffered saline, pH 7.4, containing 15 mM sodium azide.


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
DHCR24 gene expression is upregulated in melanoma metastases and associated to resistance to oxidative stress-induced apoptosis
Di Stasi D, et al.
International Journal of Cancer. Journal International Du Cancer, 115(2), 224-230 (2005)
The human homolog of Diminuto/Dwarf1 gene (hDiminuto): a novel ACTH-responsive gene overexpressed in benign cortisol-producing adrenocortical adenomas
Sarkar D, et al.
J. Clin. Endocr., 86(11), 5130-5137 (2001)
The role of seladin-1/DHCR24 in cholesterol biosynthesis, APP processing and Abeta generation in vivo
Crameri A, et al.
The Embo Journal, 25(2), 432-443 (2006)
Regulation of cellular response to oncogenic and oxidative stress by Seladin-1
Wu C, et al.
Nature, 432(7017), 640-640 (2004)
Expression of the novel adrenocorticotropin-responsive gene selective Alzheimer?s disease indicator-1 in the normal adrenal cortex and in adrenocortical adenomas and carcinomas
Luciani P, et al.
The Journal of Clinical Endocrinology and Metabolism, 89(3), 1332-1339 (2004)

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