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Merck

P5622

Sigma-Aldrich

Anti-Pen-2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

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.

Specificity

Anti-PEN2 antibody recognizes Pen-2 (10 kDa).

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

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.

Storage and Stability

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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