α-Parvin Antibody [P1L24] | Primary Antibodies

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

Lane 1: Hela, Lane 2: COS-7, Lane 3: NIH/3T3, Lane 4: C6

Usage Information

Dilution
WB1:1000 IP1:50 IF1:200

Application
WB, IP, IF

Reactivity
Human, Mouse, Rat, 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
50-80 kDa

Datasheet & SDS

Biological Description

Specificity
α-Parvin Antibody [P1L24] detects endogenous levels of total α-Parvin protein.

Clone
P1L24

Synonym(s)
Alpha-parvin; Actopaxin; Calponin-like integrin-linked kinase-binding protein; CH-ILKBP; PARVA

Background
α-Parvin belongs to the parvin family of adaptor proteins within the IPP (ILK/PINCH/parvin) complex that bridges integrin extracellular matrix receptors to the actin cytoskeleton at focal adhesions. α-parvin organizes two calponin-homology domains that bind F-actin alongside a paxillin-binding CH2 subdomain and ankyrin repeats that engage ILK and PINCH for ternary complex assembly at integrin tails. Upon ECM engagement, ERK-mediated N-terminal serine phosphorylation dissociates α-parvin from TESK1 cofilin kinase, relieving inhibition to enable cofilin phosphorylation, LIMK1 activation, and F-actin stabilization at lamellipodia for directional motility. α-parvin simultaneously recruits CdGAP to hydrolyze Rac1-GTP, tempering lamellipodial expansion while promoting focal adhesion turnover through paxillin-LIMK signaling that balances protrusion with traction force generation. Interaction with α-actinin cross-links actin filaments to ILK pseudokinase activity, propagating FAK/Src cascades that phosphorylate paxillin for RIPLET-mediated ubiquitination and endocytic recycling of integrin clusters during migration. α-parvin coordinates epithelial sheet migration and myofibroblast contractility in wound healing, with ubiquitous expression adapting to mechanical cues via stiffness-dependent ILK conformational shifts. During mitosis, cyclin B1-CDK1 phosphorylation modulates α-parvin localization to the spindle, linking cytoskeletal reorganization to chromosome segregation fidelity. Dysregulation elevates α-parvin in invasive carcinomas, where hyperphosphorylation sustains Rac1 hyperactivation and matrix metalloproteinase secretion for basement membrane breaching.

Background

α-Parvin belongs to the parvin family of adaptor proteins within the IPP (ILK/PINCH/parvin) complex that bridges integrin extracellular matrix receptors to the actin cytoskeleton at focal adhesions. α-parvin organizes two calponin-homology domains that bind F-actin alongside a paxillin-binding CH2 subdomain and ankyrin repeats that engage ILK and PINCH for ternary complex assembly at integrin tails. Upon ECM engagement, ERK-mediated N-terminal serine phosphorylation dissociates α-parvin from TESK1 cofilin kinase, relieving inhibition to enable cofilin phosphorylation, LIMK1 activation, and F-actin stabilization at lamellipodia for directional motility. α-parvin simultaneously recruits CdGAP to hydrolyze Rac1-GTP, tempering lamellipodial expansion while promoting focal adhesion turnover through paxillin-LIMK signaling that balances protrusion with traction force generation. Interaction with α-actinin cross-links actin filaments to ILK pseudokinase activity, propagating FAK/Src cascades that phosphorylate paxillin for RIPLET-mediated ubiquitination and endocytic recycling of integrin clusters during migration. α-parvin coordinates epithelial sheet migration and myofibroblast contractility in wound healing, with ubiquitous expression adapting to mechanical cues via stiffness-dependent ILK conformational shifts. During mitosis, cyclin B1-CDK1 phosphorylation modulates α-parvin localization to the spindle, linking cytoskeletal reorganization to chromosome segregation fidelity. Dysregulation elevates α-parvin in invasive carcinomas, where hyperphosphorylation sustains Rac1 hyperactivation and matrix metalloproteinase secretion for basement membrane breaching.

References
https://pubmed.ncbi.nlm.nih.gov/18508764/ https://pubmed.ncbi.nlm.nih.gov/16314921/

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%