P5622
Anti-Pen-2 antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 10 kDa
species reactivity
human
technique(s)
microarray: suitable
western blot: 3-6 μg/mL using whole extract of human kidney 293 cells expressing human Pen-2
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PSENEN(55851)
mouse ... Psen2(19165)
General description
Presenilin enhancer γ-secretase subunit (Pen-2/ PSENEN) gene, with four exons spanning 1.4 kb, is mapped to human chromosome 19q13.12. Pen-2 is an integral membrane protein with 101 amino acids. The protein is characterized with two transmembrane domains and a cytosolic loop domain, with the C- and N-termini facing the lumen of the endoplasmic reticulum.
Immunogen
synthetic peptide encoding amino acids 86-101 located at the C-terminus of human pen-2, conjugated to KLH. This sequence is identical in mouse pen-2.
Application
Anti-Pen-2 antibody produced in rabbit has been used in immunoblotting.
Biochem/physiol Actions
Anti-PEN2 antibody recognizes Pen-2 (10 kDa).
Pen-2 is a critical component of the presenilin (PS)1/γ-secretase and PS2/γsecretase complexes. siRNA interference mediated down regulation of pen-2 is due to reduced PS levels, impaired nicastrin (Nct) maturation and deficient γ secretase complex formation. Pen-2 preferentially interacts with PS1 and induce PS1 endoproteolysis. In addition, it also stabilizes PS fragment heterodimer within the γ-secretase complex subsequent to PS endoproteolysis. PEN-2 plays a vital role in γ-secretase complex maturation in the absence of PS endoproteolysis. Mutation in the PEN-2 gene leads to the development of familial comedones syndrome.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
For continuous use, store at 2-8 °C for up to one month. For extended storage freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
Disclaimer
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.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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A frameshift mutation in PEN-2 causes familial comedones syndrome
Panmontha W, et al.
Dermatology (Basel, Switzerland), 231(1), 77-81 (2015)
Requirement of PEN-2 for stabilization of the presenilin N-/C-terminal fragment heterodimer within the $\gamma$-secretase complex
Prokop S, et al.
The Journal of Biological Chemistry, 279(22), 23255-23261 (2004)
Dopamine D2 receptor and $\beta$-arrestin 2 mediate Amyloid-$\beta$ elevation induced by anti-parkinson?s disease drugs, levodopa and piribedil, in neuronal cells
Lu J, et al.
PLoS ONE, 12(3), e0173240-e0173240 (2017)
Wen-jie Luo et al.
The Journal of biological chemistry, 278(10), 7850-7854 (2003-01-11)
Presenilin (PS, PS1/PS2) complexes are known to be responsible for the intramembranous gamma-secretase cleavage of the beta-amyloid precursor protein and signaling receptor Notch. PS holoprotein undergoes endoproteolysis by an unknown enzymatic activity to generate NH(2)- and COOH-terminal fragments, a process
Harald Steiner et al.
The Journal of biological chemistry, 277(42), 39062-39065 (2002-08-29)
The Alzheimer disease-associated presenilin (PS) proteins apparently provide the active site of gamma-secretase, an unusual intramembrane-cleaving aspartyl protease. PSs principally occur as high molecular weight protein complexes that contain nicastrin (Nct) and additional so far unidentified components. Recently, PEN-2 has
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