Profilin-1 Antibody [P24C16] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Hamster, Monkey, Dog

Lane 1: Hela, Lane 2: COS, Lane 3: C6, Lane 4: CHO

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, Mouse, Rat, Hamster, Monkey, Dog

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
15 kDa

Datasheet & SDS

Biological Description

Specificity
Profilin-1 Antibody [P24C16] detects endogenous levels of total Profilin-1 protein.

Clone
P24C16

Synonym(s)
Profilin-1; Epididymis tissue protein Li 184a; Profilin I; PFN1

Background
Profilin-1 serves as the ubiquitously expressed member of the profilin family of actin-monomer binding proteins, acting as a central regulator of actin cytoskeleton dynamics essential for cellular motility, division, and adhesion. It features a compact globular fold with distinct actin-binding, polyproline ligand (PLP), and phosphoinositide-binding sites that enable G-actin sequestration and nucleotide exchange from ADP to ATP states. Profilin-1 delivers ATP-G-actin to the barbed ends of growing filaments while discriminating against spontaneous nucleation, preferentially channeling monomers to Ena/VASP and formin pathways over Arp2/3 complex assembly; this creates homeostatic balance by inhibiting Arp2/3-driven lamellipodia while promoting VASP-mediated leading-edge protrusion through adhesion-dependent PKA-regulated interactions that enhance F-actin accumulation without altering total cellular levels. Profilin-1 also binds polyproline motifs in palladin and dynamin-1 to coordinate actin-membrane remodeling and endocytosis, with phosphorylation at S137 fine-tuning affinity for PLP partners like VASP to sustain directional migration. Profilin-1 governs embryonic cleavage and blastocyst formation by ensuring actin flux for cytokinesis and polarity, while in migrating cells, it dictates protrusion-retraction cycles critical for immune surveillance and wound healing, making it ideal for researchers probing actin pathway competition where isoform redundancy reveals context-specific roles. Dysregulation through depletion elevates Arp2/3 activity, disrupts homeostasis, and triggers embryonic lethality by the 2-cell stage, while mutations impair neuronal trafficking in ALS contexts.

Background

Profilin-1 serves as the ubiquitously expressed member of the profilin family of actin-monomer binding proteins, acting as a central regulator of actin cytoskeleton dynamics essential for cellular motility, division, and adhesion. It features a compact globular fold with distinct actin-binding, polyproline ligand (PLP), and phosphoinositide-binding sites that enable G-actin sequestration and nucleotide exchange from ADP to ATP states. Profilin-1 delivers ATP-G-actin to the barbed ends of growing filaments while discriminating against spontaneous nucleation, preferentially channeling monomers to Ena/VASP and formin pathways over Arp2/3 complex assembly; this creates homeostatic balance by inhibiting Arp2/3-driven lamellipodia while promoting VASP-mediated leading-edge protrusion through adhesion-dependent PKA-regulated interactions that enhance F-actin accumulation without altering total cellular levels. Profilin-1 also binds polyproline motifs in palladin and dynamin-1 to coordinate actin-membrane remodeling and endocytosis, with phosphorylation at S137 fine-tuning affinity for PLP partners like VASP to sustain directional migration. Profilin-1 governs embryonic cleavage and blastocyst formation by ensuring actin flux for cytokinesis and polarity, while in migrating cells, it dictates protrusion-retraction cycles critical for immune surveillance and wound healing, making it ideal for researchers probing actin pathway competition where isoform redundancy reveals context-specific roles. Dysregulation through depletion elevates Arp2/3 activity, disrupts homeostasis, and triggers embryonic lethality by the 2-cell stage, while mutations impair neuronal trafficking in ALS contexts.

References
https://pubmed.ncbi.nlm.nih.gov/25543281/ https://pubmed.ncbi.nlm.nih.gov/24385538/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%