PSENEN Antibody, Biotin conjugated
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Description
Introduction to PSENEN Antibody, Biotin Conjugated
The PSENEN Antibody, Biotin conjugated is a chemically modified immunoglobulin designed to detect Presenilin Enhancer Gamma-Secretase Subunit (PSENEN), a critical component of the γ-secretase complex. This conjugate leverages biotin's high-affinity binding to streptavidin, enabling amplified detection in assays like ELISA, Western blotting, and immunohistochemistry (IHC) . PSENEN, also known as PEN-2, regulates γ-secretase activity, which processes amyloid-β (Aβ) peptides linked to Alzheimer’s disease (AD) pathogenesis .
Key Features:
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Target: PSENEN (UniProt: Q9NZ42).
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Conjugate: Biotin, facilitating signal amplification via streptavidin-HRP or streptavidin-AP systems .
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Applications: Research into AD, Notch signaling, and γ-secretase modulators .
Structure and Function of PSENEN
PSENEN stabilizes the γ-secretase complex, consisting of presenilin (PSEN1/PSEN2), nicastrin, and APH-1 . Its conserved DYSLF motif in the C-terminus is essential for complex assembly and Aβ42/Aβ40 ratio modulation . Mutations in PSENEN are associated with familial acne inversa and early-onset AD .
Mechanism:
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Primary Antibody Binding: Biotinylated PSENEN antibody binds target protein.
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Secondary Reagent: Streptavidin-HRP or streptavidin-AP conjugate binds biotin, enabling enzymatic detection (e.g., TMB substrate for colorimetric assays) .
Advantages:
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Signal Amplification: Streptavidin’s high affinity (Kd ≈ 10⁻¹⁵ M) enhances detection of low-abundance PSENEN .
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Versatility: Compatible with ELISA, Western blotting, and IHC protocols .
Applications in Research
γ-Secretase Modulation
PSENEN regulates Aβ42/Aβ40 ratios, a therapeutic target in AD. A γ-secretase modulator binds PSENEN, reducing Aβ42 production .
Knockout Studies
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Psenen−/− Fibroblasts: Show abolished Aβ40/42 generation and APP CTF accumulation, confirming PSENEN’s essential role in γ-secretase activity .
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Cysteine Scanning: E49C mutant reacts with TS-XX-biotin, highlighting PSENEN’s extracellular topology .
Cross-Linking Experiments
SPDP cross-linker identifies proximity between PSENEN’s loop and PSEN1 CTF, supporting direct interactions in the active complex .
Challenges and Considerations
Product Specs
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
We typically dispatch products within 1-3 business days of receiving your order. Delivery times may vary depending on the chosen shipping method and location. Please consult your local distributors for specific delivery timeframes.
Synonyms
PSENEN; PEN2; MDS033; Gamma-secretase subunit PEN-2; Presenilin enhancer protein 2
Target Names
Uniprot No.
Target Background
Function
PSENEN is an essential 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). The gamma-secretase complex is involved in Notch and Wnt signaling cascades, regulating downstream processes through its role in processing key regulatory proteins, and potentially by modulating cytosolic CTNNB1 levels. PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity.
Gene References Into Functions
- High gamma-secretase expression has been linked to head and neck squamous cell carcinoma. PMID: 29047105
- Studies have shown that APP substrate occupancy of three specific pockets within the gamma-secretase complex occurs after initial substrate binding, but before catalysis. This suggests that a conformational change in the substrate may be necessary for cleavage. PMID: 27580372
- Mutations in PSENEN have been associated with a co-occurrence of Dowling-Degos disease and acne inversa (AI), likely triggered by predisposing factors for AI. PMID: 28287404
- Zinc and copper have been shown to inhibit Abeta production by directly targeting the presenilin and nicastrin subunits of the gamma-secretase complex. PMID: 28096459
- PSENEN may play a critical role in the progression of atopic dermatitis by participating in the Notch signaling pathway. PMID: 26967585
- PEN-2, along with nicastrin, has been identified as an additional substrate-binding subunit. PMID: 27220847
- Research suggests that the deltaOR-Phe27Cys variation modulates beta- and gamma-secretase activity in late-stage Alzheimer's disease, possibly through post-translational mechanisms. PMID: 26402014
- TRPC6 has been found to interact specifically with APP, leading to inhibition of its cleavage by gamma-secretase and a reduction in Abeta production. PMID: 26581893
- Secondary mutations in presenilin 1 alone have been observed to activate gamma-secretase activity. PMID: 26559975
- Both human PS2V and zebrafish PS1IV have been shown to stimulate gamma-secretase activity despite significant structural differences. PMID: 25814654
- Studies indicate that familial Alzheimer's disease (FAD) and control brain samples exhibit similar overall gamma-secretase activity levels. Therefore, loss of overall gamma-secretase function may not be a crucial component of the pathogenic mechanism. PMID: 26481686
- PEN-2 has been identified as the causative gene for familial comedones. PMID: 26044244
- The first hydrophobic domain of Pen-2 forms a structure resembling a reentrant loop, while the second hydrophobic domain spans the lipid bilayer. PMID: 26296997
- Shedding of BCMA by gamma-secretase controls plasma cells in the bone marrow and represents a potential biomarker for B-cell involvement in human autoimmune diseases. PMID: 26065893
- Tumor necrosis factor-alpha and interleukin-10 levels were found to be elevated in acne inversa patients with nicastrin or presenilin enhancer mutations. PMID: 26067312
- SLC2A13 has been identified as a novel gamma-secretase associated protein that regulates amyloid beta production without affecting Notch cleavage. PMID: 26094765
- Brain proteins have been identified that exhibit neuron-specific interactions with gamma-secretase. PMID: 25893612
- A complete inhibition of PS1-induced apoptosis was achieved by knockdown of PS1-associated protein (PSAP), a mitochondrial proapoptotic protein that forms a complex with Bax upon induction of apoptosis, in the presence of a gamma-secretase inhibitor. PMID: 26025363
- Research focuses on analyzing how the conformation of presenilin, Pen-2, Aph-1, and nicastrin impact the function and mechanism of gamma-secretase. PMID: 25918421
- Mutation of the AXXXAXXXG motifs on PS1 and PS2 has been shown to significantly affect gamma-secretase activity. PMID: 25614624
- Presenilin 1 (PS1), the catalytic subunit of gamma-secretase, contains an initial substrate-binding site distinct from the catalytic site. PMID: 25673856
- Recombinant human Pen-2 fusion protein has been purified from bacteria to greater than 95% purity. PMID: 24865334
- Findings suggest that iron can increase gamma-secretase activity by promoting the level of FTL, which interacts with and stabilizes PEN-2. PMID: 23685131
- A review of mutations in the gamma-secretase genes NCSTN, PSENEN, and PSEN1, and the role of gamma-secretase in cutaneous biology, specifically in hidradenitis suppurativa, has been conducted. PMID: 23096707
- Allele A of the Pen 2 gene may increase the risk of late-onset Alzheimer's disease. PMID: 23134962
- A 269 bp region located between the PSENEN and U2AF1L4 human genes has been identified as a bidirectional promoter regulating the coordinated divergent transcription of these genes. PMID: 23246698
- Mutations in the gamma-secretase genes NCSTN, PSENEN, and PSEN1 have been found to underlie rare forms of hidradenitis suppurativa (acne inversa). PMID: 22622421
- The molecular state of gamma-secretase and its enzymological characteristics have been described. PMID: 22787762
- Secretase subunits restrict the arrangement of presenilin's transmembrane domains during the formation of the functional structure of the catalytic pore. PMID: 22689582
- Research suggests that gradual saturation of gamma-secretase with its substrate may be the pathogenic process in various alleged causes of Alzheimer's disease (AD). PMID: 22479317
- Expression of calsenilin leads to a disruption of presenilin 1/gamma-secretase-mediated epsilon-cleavage of N-cadherin, resulting in the significant accumulation of N-cadherin C-terminal fragment 1. PMID: 21852538
- NCSTN and PSENEN have been implicated in the pathogenesis of some familial hidradenitis suppurativa (Acne Inversa). PMID: 21412258
- Structural analysis of PEN-2 conformation has been conducted using single-particle electron microscopy. PMID: 21454611
- Research supports a gamma-secretase-independent role of presenilin-1 in the modulation of filamin-mediated actin cytoskeleton. PMID: 20847418
- A study found independent loss-of-function mutations in PSENEN, PSEN1, or NCSTN in six Chinese acne inversa (AI) families. This research identifies the gamma-secretase component genes as causative factors for a subset of familial AI. PMID: 20929727
- Data indicates that intramembranous cleavage by gamma-secretase and related intramembrane-cleaving proteases may generally occur through a stepwise endoproteolysis process. PMID: 20534834
- Hematopoietic gamma-secretase has been observed to have reduced activity for APP and Notch1 processing compared to epithelial gamma-secretase. PMID: 20178366
- Transactivation of the Pen2 promoter by presenilin 1/2 is p53-dependent. PMID: 19889971
- PEN-2 is a component of the gamma-secretase complex. PMID: 12198112
- PEN-2 plays a role in regulating the proteolytic processing of presenilin 1 in conjunction with APH-1. PMID: 12522139
- Research has examined the membrane topology of PEN-2. PMID: 12639958
- APH-1 stabilizes the presenilin holoprotein within the complex, while PEN-2 is essential for endoproteolytic processing of presenilin and conferring gamma-secretase activity to the complex. PMID: 12660785
- Expression of PEN2 has been found to increase amyloid beta peptide levels and gamma-secretase activity. PMID: 12763021
- Presenilin 1 (PS1)-derived fragments, mature nicastrin, APH-1, and PEN-2 associate with cholesterol-rich detergent-insoluble membrane (DIM) domains in both non-neuronal cells and neurons. PMID: 15322084
- The sequence and length of the C terminus of PEN-2 are crucial for intermolecular interactions and the function of presenilin complexes. PMID: 15322109
- The presenilin-subunit stabilizing function of PEN-2 is dependent on the length and overall sequence of its carboxyl-terminal domain. PMID: 15953349
- Knockdown of ubiquilin-1 and -2 protein expression using RNAi (RNA interference) has been observed to increase Pen-2 and nicastrin levels. PMID: 15975090
- Mutational analyses have revealed that the "NF" sequence within the TMD4 of PS1 is the minimal motif required for binding with PEN-2, promoting PS1 endoproteolysis and gamma-secretase activity. PMID: 16234243
- Pen-2 may contribute to the activation of the gamma-secretase complex by directly binding to the TMD4 of PS1. PMID: 16234244
- COX-2 may be a downstream effector of mutant N141I PS2-mediated apoptotic cell death, and inhibition of COX-2 may offer neuroprotection in AD by modulating a GSK-3beta-beta-catenin-mediated response. PMID: 16331303
Database Links
Involvement In Disease
Acne inversa, familial, 2 (ACNINV2)
Protein Families
PEN-2 family
Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Tissue Specificity
Widely expressed. Expressed in leukocytes, lung, placenta, small intestine, liver, kidney, spleen thymus, skeletal muscle, heart and brain.
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