Desmin Antibody [G12C10]

Catalog No.: F4603

Application: Reactivity: Human, Mouse, Rat

Lane 1: C2C12, Lane 2: Rat heart, Lane 3: human heart

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
WB1:1000 IF1:100

Application
WB, IF

Source
Rabbit Monoclonal Antibody

Reactivity
Human, Mouse, Rat

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
53 kDa

Datasheet & SDS

生物学的記述

Specificity
Desmin Antibody [G12C10] detects endogenous levels of total Desmin protein.

Clone
G12C10

Synonym(s)
Desmin; DES

Background
Desmin is a muscle-specific type III intermediate filament protein expressed exclusively in cardiac, skeletal, and smooth muscle cells, providing cytoskeletal structural integrity. Desmin features a tripartite organization: a variable N-terminal globular head domain (dynamic α-helices/β-sheets with R16/S32 for protein binding), a central conserved α-helical rod domain (308 aa) with four coiled-coil segments (1A, 1B, 2A, 2B) connected by linkers (L1, L12), and a C-terminal tail domain enabling lateral filament assembly. Desmin polymerizes into networks linking Z-disks, myofibrils, nuclei, mitochondria (via NDUFS2), and lysosomes (via saposin D), transmitting mechanical force during contraction, maintaining sarcomere alignment, and coordinating with actin/myosin/dystrophin/synemin/αB-crystallin through head domain three-helix bundles stabilized by hydrophobic/hydrogen bonds. It ensures organelle positioning and cellular resilience to stress via dynamic head-tail protrusions. Mutations (e.g., in rod domain) disrupt polymerization/aggregation, causing desmin-related myopathies (DRM), cardiomyopathies with muscle weakness, and protein aggregates.

Background

Desmin is a muscle-specific type III intermediate filament protein expressed exclusively in cardiac, skeletal, and smooth muscle cells, providing cytoskeletal structural integrity. Desmin features a tripartite organization: a variable N-terminal globular head domain (dynamic α-helices/β-sheets with R16/S32 for protein binding), a central conserved α-helical rod domain (308 aa) with four coiled-coil segments (1A, 1B, 2A, 2B) connected by linkers (L1, L12), and a C-terminal tail domain enabling lateral filament assembly. Desmin polymerizes into networks linking Z-disks, myofibrils, nuclei, mitochondria (via NDUFS2), and lysosomes (via saposin D), transmitting mechanical force during contraction, maintaining sarcomere alignment, and coordinating with actin/myosin/dystrophin/synemin/αB-crystallin through head domain three-helix bundles stabilized by hydrophobic/hydrogen bonds. It ensures organelle positioning and cellular resilience to stress via dynamic head-tail protrusions. Mutations (e.g., in rod domain) disrupt polymerization/aggregation, causing desmin-related myopathies (DRM), cardiomyopathies with muscle weakness, and protein aggregates.

References
[1] Vlachakis D, et al. Cells. 2024 Mar 29;13(7):603. [2] Costa ML, et al. Braz J Med Biol Res. 2004 Dec;37(12):1819-30.

PVDFメンブレン孔径参考表

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%