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AB78914

Anti-Presenilin 1/PS-1 (phospho S357) antibody

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(3 Publications)

Rabbit Polyclonal Presenilin 1/PS-1 phospho S357 antibody. Suitable for WB, IHC-P and reacts with Mouse, Human samples. Cited in 3 publications. Immunogen corresponding to Synthetic Peptide within Human PSEN1 phospho S357.

View Alternative Names

AD3, PS1, PSNL1, PSEN1, Presenilin-1, PS-1, Protein S182

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Presenilin 1/PS-1 (phospho S357) antibody (AB78914)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Presenilin 1/PS-1 (phospho S357) antibody (AB78914)

ab78914 at 1/50 dilution staining Presenilin 1/PS-1 in human brain by Immunohistochemistry using paraffin-embedded tissue, in the absence or presence of the immunising phosphopeptide.

Western blot - Anti-Presenilin 1/PS-1 (phospho S357) antibody (AB78914)
  • WB

Unknown

Western blot - Anti-Presenilin 1/PS-1 (phospho S357) antibody (AB78914)

All lanes:

Western blot - Anti-Presenilin 1/PS-1 (phospho S357) antibody (ab78914) at 1/500 dilution

Lane 1:

RAW264.7 cell extracts, treated with UV (5mins) at 30 µg

Lane 2:

RAW264.7 cell extracts, treated with UV (5mins) at 30 µg with immunising phosphopeptide

Predicted band size: 53 kDa

Observed band size: 46 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human PSEN1 phospho S357. The exact immunogen used to generate this antibody is proprietary information.

P49768

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab78914 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Supplementary information

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

Presenilin 1 often referred to as PS-1 is a protein with an important role in the function of gamma-secretase a multi-subunit protease complex. It weighs approximately 50 kDa and is widely expressed in different tissues especially in the brain. Presenilin 1 functions as part of the gamma-secretase complex which is responsible for processing several type I transmembrane proteins. This protein undergoes endoproteolytic processing to form an N-terminal and C-terminal fragment which are pivotal for its gamma-secretase activity.
Biological function summary

Presenilin 1 plays a fundamental role in the cleavage of amyloid precursor protein (APP) within the transmembrane domain. This cleavage results in the formation of amyloid-beta peptides which are of significant interest in neurobiology. Presenilin 1 is an integral component of the gamma-secretase complex that includes nicastrin APH-1 and PEN-2. This complex involvement underlines the enzyme's importance in cell signaling pathways and modulation of synaptic functions. The functionality at the synaptic level is particularly important given its expression pattern and involvement in neural processes.

Pathways

The action of presenilin 1 is closely linked to the Notch signaling pathway and the amyloidogenic pathway. Presenilin 1 facilitates the intramembrane cleavage of the Notch receptor releasing the Notch intracellular domain that translocates to the nucleus and affects gene transcription. The protein's role in processing APP into amyloid-beta peptides links it directly to Alzheimer's disease pathology. The protein Tax also a component of the gamma-secretase complex shows interdependencies in these pathways.

Presenilin 1 holds significant relevance in Alzheimer's disease where mutations in its gene are associated with early-onset familial Alzheimer's. The production of amyloid-beta peptides through presenilin 1's interaction with APP is central to the disease's pathogenesis. Another disorder linked to presenilin 1 is Dilated Cardiomyopathy where presenilin mutations may affect calcium signaling in cardiac cells. In Alzheimer's the interaction between presenilin 1 and the amyloid-beta peptide protein is critical while in cardiac issues it's more about protein misfolding and signaling mishaps.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) (PubMed : 10206644, PubMed : 10545183, PubMed : 10593990, PubMed : 10811883, PubMed : 10899933, PubMed : 12679784, PubMed : 12740439, PubMed : 15274632, PubMed : 20460383, PubMed : 25043039, PubMed : 26280335, PubMed : 28269784, PubMed : 30598546, PubMed : 30630874). Requires the presence of the other members of the gamma-secretase complex for protease activity (PubMed : 15274632, PubMed : 25043039, PubMed : 26280335, PubMed : 30598546, PubMed : 30630874). Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (PubMed : 10593990, PubMed : 10811883, PubMed : 10899933, PubMed : 9738936). Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin) (PubMed : 11953314). Under conditions of apoptosis or calcium influx, cleaves CDH1 (PubMed : 11953314). This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling (PubMed : 11953314, PubMed : 9738936). Required for normal embryonic brain and skeleton development, and for normal angiogenesis (By similarity). Mediates the proteolytic cleavage of EphB2/CTF1 into EphB2/CTF2 (PubMed : 17428795, PubMed : 28269784). The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is therefore involved in calcium homeostasis (PubMed : 16959576, PubMed : 25394380). Involved in the regulation of neurite outgrowth (PubMed : 15004326, PubMed : 20460383). Is a regulator of presynaptic facilitation, spike transmission and synaptic vesicles replenishment in a process that depends on gamma-secretase activity. It acts through the control of SYT7 presynaptic expression (By similarity).
See full target information PSEN1 phospho S357

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Cell communication and signaling : CCS 21:160 PubMed37370115

2023

Macrophage PTEN controls STING-induced inflammation and necroptosis through NICD/NRF2 signaling in APAP-induced liver injury.

Applications

Unspecified application

Species

Unspecified reactive species

Tao Yang,Xiaoye Qu,Jiaying Zhao,Xiao Wang,Qian Wang,Jingjing Dai,Chuanlong Zhu,Jun Li,Longfeng Jiang

Journal of applied toxicology : JAT 42:285-294 PubMed34133789

2021

The neuroprotective effects of alpha-lipoic acid on an experimental model of Alzheimer's disease in PC12 cells.

Applications

Unspecified application

Species

Unspecified reactive species

Xinrong Pei,Fangyan Hu,Feiya Luo,Xianglu Huang,Xiaoling Li,Shuxia Xing,Dingxin Long

Nature neuroscience 18:1077-80 PubMed26120963

2015

Nuclear pore complex remodeling by p75(NTR) cleavage controls TGF-β signaling and astrocyte functions.

Applications

Unspecified application

Species

Unspecified reactive species

Christian Schachtrup,Jae Kyu Ryu,Könül Mammadzada,Abdullah S Khan,Peter M Carlton,Alex Perez,Frank Christian,Natacha Le Moan,Eirini Vagena,Bernat Baeza-Raja,Victoria Rafalski,Justin P Chan,Roland Nitschke,Miles D Houslay,Mark H Ellisman,Tony Wyss-Coray,Jorge J Palop,Katerina Akassoglou
View all publications

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