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Key Documents

AB5308

Sigma-Aldrich

Anti-Presenilin-1 Antibody, loop, a.a. 275-367, CT

serum, Chemicon®

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

hamster, human, mouse, monkey

manufacturer/tradename

Chemicon®

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... PSEN1(5663)

Specificity

Presenilin-1, Loop.

Immunogen

Epitope: loop, a.a. 275-367, C-terminus
Human Presenilin-1 (amino acids 275-367) fused to C-terminus of maltose binding protein.

Application

Anti-Presenilin-1 Antibody, loop, a.a. 275-367, C-terminus is an antibody against Presenilin-1 for use in IP, WB & IC.
Immunocytochemistry: Cos7, SY5Y cell lines.

Western blot: 1:500-1:3000

Immunoprecipitation.

Optimal working dilutions must be determined by end user.

Physical form

Rabbit serum. Liquid in PBS with 0.01% sodium azide.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Hanna Laudon et al.
Journal of neurochemistry, 89(1), 44-53 (2004-03-20)
The enzyme gamma-secretase catalyzes the intramembrane proteolytic cleavage that generates the amyloid beta-peptide from the beta-amyloid precursor protein. The presenilin (PS) protein is one of the four integral membrane protein components of the mature gamma-secretase complex. The PS protein is
Theodore A Sarafian et al.
Journal of neuroscience research, 95(9), 1871-1887 (2017-01-25)
The α-synuclein protein exists in vivo in a variety of covalently modified and aggregated forms associated with Parkinson's disease (PD) pathology. However, the specific proteoform structures involved with neuropathological disease mechanisms are not clearly defined. Since α-synuclein plays a role
Lisa Placanica et al.
Biochemistry, 49(13), 2796-2804 (2010-02-25)
Gamma-secretase is a widely expressed multisubunit enzyme complex which is involved in the pathogenesis of Alzheimer disease and hematopoietic malignancies through its aberrant processing of the amyloid precursor protein (APP) and Notch1, respectively. While gamma-secretase has been extensively studied, there
Arnaldo Parra-Damas et al.
Scientific reports, 7(1), 18004-18004 (2017-12-23)
Gene expression mediated by the transcription factor cAMP-responsive element-binding protein (CREB) is essential for a wide range of brain processes. The transcriptional coactivartor CREB-regulated transcription coactivator-1 (CRTC1) is required for efficient induction of CREB target genes during neuronal activity. However, the mechanisms regulating induction of specific CREB/CRTC1-dependent
Marcella M Authiat et al.
Neural plasticity, 2022, 3172861-3172861 (2022-03-04)
Recently, we showed that DNA double-strand breaks (DSBs) are increased by the Aβ 42-amyloid peptide and decreased by all-trans retinoic acid (RA) in SH-SY5Y cells and C57BL/6J mice. The present work was aimed at investigating DSBs in cells and murine

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