ALP Antibody (Rabbit mAb) [B19A18]

Application: Reactivity: Human

Usage Information

Dilution
WB1:500-1:1000 IHC1:1000

Application
WB, IHC

Reactivity
Human

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 Observed MW
39 kDa 43 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
ALP Antibody (Rabbit mAb) [B19A18] detects endogenous levels of total ALP protein.

Clone
B19A18

Synonym(s)
ALP, PDLIM3, PDZ and LIM domain protein 3, Actinin-associated LIM protein, Alpha-actinin-2-associated LIM protein

Background
ALP belongs to the PDZ-LIM family of actin-associated scaffold proteins, structurally defined by an N-terminal PDZ domain and a C-terminal LIM domain that together mediate direct binding to α-actinin. ALP colocalizes with α-actinin at the Z-discs of striated muscle, where the PDZ-LIM architecture links the protein to the actin-binding surface of the α-actinin spectrin-repeat region, positioning ALP as a structural scaffold rather than an enzymatic regulator. ALP expression rises sharply during myogenic differentiation, and disruption of ALP expression reduces transcript levels of the muscle regulatory factors myogenin and MyoD, placing ALP function upstream of the core myogenic transcriptional program. Loss of ALP causes a marked reduction in organized actin filament bundles within differentiating muscle cells, and this cytoskeletal disruption directly suppresses the activity of serum response factor, a transcription factor whose activation depends on actin polymerization state and the nuclear availability of its coactivator MAL. Restoring MyoD expression in ALP-depleted cells is sufficient to rescue myogenic differentiation despite persistent actin bundle loss, indicating that ALP acts through the actin-SRF-MyoD axis to control entry into the differentiation program rather than through a parallel independent pathway. Treatment with an actin-stabilizing compound restores SRF activity and differentiation capacity in ALP-depleted cells, reinforcing that ALP's contribution to myogenesis operates through maintenance of filamentous actin architecture. PDZ-LIM family members, including ALP, interact with the CH and spectrin-repeat domains of α-actinin isoforms across muscle and non-muscle contexts, supporting roles in both Z-disc stability and, in emerging evidence, actin-dependent membrane trafficking. Z-disc scaffold proteins of this family, including ALP, are implicated in the structural integrity of cardiac and skeletal sarcomeres, with disruption linked to cardiomyopathy susceptibility in genetic association studies.

Background

ALP belongs to the PDZ-LIM family of actin-associated scaffold proteins, structurally defined by an N-terminal PDZ domain and a C-terminal LIM domain that together mediate direct binding to α-actinin. ALP colocalizes with α-actinin at the Z-discs of striated muscle, where the PDZ-LIM architecture links the protein to the actin-binding surface of the α-actinin spectrin-repeat region, positioning ALP as a structural scaffold rather than an enzymatic regulator. ALP expression rises sharply during myogenic differentiation, and disruption of ALP expression reduces transcript levels of the muscle regulatory factors myogenin and MyoD, placing ALP function upstream of the core myogenic transcriptional program. Loss of ALP causes a marked reduction in organized actin filament bundles within differentiating muscle cells, and this cytoskeletal disruption directly suppresses the activity of serum response factor, a transcription factor whose activation depends on actin polymerization state and the nuclear availability of its coactivator MAL. Restoring MyoD expression in ALP-depleted cells is sufficient to rescue myogenic differentiation despite persistent actin bundle loss, indicating that ALP acts through the actin-SRF-MyoD axis to control entry into the differentiation program rather than through a parallel independent pathway. Treatment with an actin-stabilizing compound restores SRF activity and differentiation capacity in ALP-depleted cells, reinforcing that ALP's contribution to myogenesis operates through maintenance of filamentous actin architecture. PDZ-LIM family members, including ALP, interact with the CH and spectrin-repeat domains of α-actinin isoforms across muscle and non-muscle contexts, supporting roles in both Z-disc stability and, in emerging evidence, actin-dependent membrane trafficking. Z-disc scaffold proteins of this family, including ALP, are implicated in the structural integrity of cardiac and skeletal sarcomeres, with disruption linked to cardiomyopathy susceptibility in genetic association studies.

References
https://pubmed.ncbi.nlm.nih.gov/38095060/ https://pubmed.ncbi.nlm.nih.gov/17332502/

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

Tech Support

Handling Instructions

Tel: +1-832-582-8158 Ext:3

If you have any other enquiries, please leave a message.

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%