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P7624

Sigma-Aldrich

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

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

Synonym(s):

Anti-PFN1

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About This Item

MDL number:
MFCD09265368
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~15 kDa

species reactivity

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

UniProt accession no.

P15735

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

Related Categories

General description

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.

Immunogen

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

Biochem/physiol Actions

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.

Target description

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

Physical form

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

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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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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