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P0084

Sigma-Aldrich

Monoclonal Anti-Pinin antibody produced in mouse

~1.5 mg/mL, clone 5F1, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-DRS, Anti-PNN, Anti-SDK3, Anti-memA

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

5F1, monoclonal

form

buffered aqueous solution

mol wt

antigen ~140 kDa

species reactivity

monkey, bovine, human, canine

packaging

antibody small pack of 25 μL

concentration

~1.5 mg/mL

technique(s)

immunocytochemistry: suitable
indirect ELISA: suitable
western blot: 1-2 μg/mL using HeLa nuclear cell extract

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PNN(5411)

General description

Monoclonal Anti-Pinin (mouse IgG1 isotype) is derived from the hybridoma 5F1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. Pinin (PNN) is a serine/arginine-rich (SR)-related protein, that is found to localize to the cytoplasmic face of the desmosomal plaque in the convergence of intermediate filaments and to pin them to the desmosome. It consists of an Arg-Ser (RS) domain in its carboxyl terminus. This gene is mapped to human chromosome 14q.

Specificity

Monoclonal Anti-Pinin recognizes human pinin. It crossreacts with monkey, bovine, and dog pinin.

Immunogen

synthetic peptide corresponding to amino acids 547-737 of human pinin, conjugated to KLH.

Application

Monoclonal Anti-Pinin antibody produced in mouse may be used in:
  • enzyme-linked immunosorbent assay (ELISA)
  • immunoblotting
  • immunocytochemistry

Biochem/physiol Actions

Pinin (PNN) is mainly linked with the mature desmosomes of the epithelia. It plays a role in inducing junction formation and enhance cell aggregation. PNN transcription and protein levels were found to be reduced in renal and transitional cell carcinomas, suggesting its role as a tumor suppressor. PNN protein reduction by RNAi or knockdown resulted in loss of cell-cell adhesion as well as aberrant mouse development. It plays a key role in mRNA export, cell−cell adhesion, alternative splicing and cell migration. PNN also controls gene transcription.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For extended storage, freeze at -20 °C in working aliquots. Repeated freezing and thawing, or 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 notused 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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Certificates of Analysis (COA)

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Loss of Pnn expression results in mouse early embryonic lethality and cellular apoptosis through SRSF1-mediated alternative expression of Bcl-xS and ICAD
Leu S, et al.
Journal of Cell Science, 125(13), 3164-3172 (2012)
Alvin Wong et al.
Plastic and reconstructive surgery, 130(5), 1012-1021 (2012-10-26)
Infantile hemangiomas can cause significant morbidity during proliferation, yet there is no U.S. Food and Drug Administration-approved treatment. They are believed to form from hemangioma stem cells, which differentiate toward a hemangioma endothelial cell phenotype. Recently, propranolol has demonstrated effectiveness
Change in gene expression subsequent to induction of Pnn/DRS/memA: increase in p21 cip1/waf1
Shi Y, et al.
Oncogene, 20(30), 4007-4018 (2001)
Reduction of Pnn by RNAi induces loss of cell-cell adhesion between human corneal epithelial cells
Joo JH, et al.
Molecular Vision, 11(1), 133-142 (2005)
Xuanming Hu et al.
BMC complementary and alternative medicine, 17(1), 329-329 (2017-06-24)
Gastrointestinal motility disorder has been demonstrated to be regulated by acupuncture treatment. The mechanisms underlying the effects of acupuncture stimulation of abdominal and lower limb acupoints on gastrointestinal motility have been thoroughly studied; however, the physiology underlying the effects of

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