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Key Documents

P7624

Sigma-Aldrich

Anti-Profilin 1 (C-terminal) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-PFN1

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~15 kDa

Espèces réactives

mouse, human, rat

Concentration

~1 mg/mL

Technique(s)

immunoprecipitation (IP): 5-10 μg using mouse NIH3T3 cell lysates
indirect immunofluorescence: 10-20 μg/mL using rat NRK cells
western blot (chemiluminescent): 1-2 μg/mL using whole extract of human HeLa cells

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PFN1(5216)
mouse ... Pfn1(18643)
rat ... Pfn1(64303)

Description générale

Profilin 1 is a ubiquitous actin monomer-binding protein. Profilin 1 is the most ubiquitous and abundant and is highly expressed throughout development and adulthood in most tissues including brain.

Immunogène

synthetic peptide corresponding to amino acid residues 128-140 of human profilin 1, conjugated to KLH. The corresponding sequence is identical in rat and mouse.

Application

Anti-Profilin 1 (C-terminal) antibody produced in rabbit has been used in:
  • immunoblotting
  • immunostaining
  • immunoprecipitation
  • immunofluorescence
  • profilin enzyme-linked immunosorbent assay (ELISA) analysis

Actions biochimiques/physiologiques

Profilin 1 is involved in actin polymerization in response to extracellular signals. Profilins were shown to be important for normal cell proliferation, differentiation and motility. Deletion of profilin 1 gene leads to an embryonic lethal phenotype. Profilin 1 is a potent regulator of actin filament dynamics. Although profilin 1 prevents spontaneous actin polymerization by complexing with unpolymerized actin in vivo, actin-profilin complexes can be added to free barbed ends, thereby stimulating actin polymerization. Profilin 1 was suggested to act as a tumor suppressor protein based on its reduced expression in several types of invasive cancers and its ability to suppress tumorigenicity when over-expressed in breast cancer cells. Deletion of profilin 1 is associated with Miller-Dieker syndrome.

Description de la cible

Profilin 1 is a ubiquitous actin monomer-binding proteininvolved in actin polymerization in response toextracellular signals.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Consulter la Bibliothèque de documents

Profilin1 Biology and its Mutation, Actin(g) in Disease
Alkam D, et al.
Cellular and Molecular Life Sciences, 74(6), 967-967 (2017)
Jitendra Kumar Kanaujiya et al.
Proteomics, 13(14), 2100-2112 (2013-04-12)
Nuclear receptor coregulators play an important role in the transcriptional regulation of nuclear receptors. In the present study, we aimed to identify estrogen receptor α (ERα) interacting proteins in Tamoxifen treated MCF7 cells. Using in vitro GST-pull down assay with
Identification of the functional profilin gene, its localization to chromosome subband 17p13. 3, and demonstration of its deletion in some patients with Miller-Dieker syndrome.
Kwiatkowski DJ, et al.
American Journal of Human Genetics, 46(3), 559-559 (1990)
Dynamic actin structures stabilized by profilin
Finkel T, et al.
Proceedings of the National Academy of Sciences of the USA, 91(4), 1510-1510 (1994)
Stefanie K Schweinhuber et al.
PloS one, 10(1), e0117244-e0117244 (2015-01-30)
The morphology of astrocytic processes determines their close structural association with synapses referred to as the 'tripartite synapse'. Concerted morphological plasticity processes at tripartite synapses are supposed to shape neuronal communication. Morphological changes in astrocytes as well as the motility

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