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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

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Synonym(s):
Anti-PFN1
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 ~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.

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.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Profilin1 Biology and its Mutation, Actin(g) in Disease
Alkam D, et al.
Cellular and Molecular Life Sciences, 74(6), 967-967 (2017)
Lisa Marie Walter et al.
Scientific reports, 11(1), 10287-10287 (2021-05-15)
Nuclear and cytoplasmic actin-cofilin rods are formed transiently under stress conditions to reduce actin filament turnover and ATP hydrolysis. The persistence of these structures has been implicated in disease pathology of several neurological disorders. Recently, the presence of actin rods

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