Recombinant Actin protein (Tagged) is a Absidia glauca Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
>85% SDS-PAGE
Escherichia coli
6x His tag N-Terminus
Myc tag C-Terminus
SDS-PAGE
No
M S M E E E I A A L V I D N G S G M C K A G F A G D D A P R A V F P S I V G R P R H Q G I M V G M G Q K D S Y V G D E A Q S K R G I L T L R Y P I E H G I V T N W D D M E K I W H H T F Y N E L R V A P E E H P V L L T E A P L N P K S N R E K M T Q I M F E T F N A P A F Y V S I Q A
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Actin-1, ACT1
Recombinant Actin protein (Tagged) is a Absidia glauca Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
>85% SDS-PAGE
Escherichia coli
6x His tag N-Terminus
Myc tag C-Terminus
SDS-PAGE
No
No
Absidia glauca
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
M S M E E E I A A L V I D N G S G M C K A G F A G D D A P R A V F P S I V G R P R H Q G I M V G M G Q K D S Y V G D E A Q S K R G I L T L R Y P I E H G I V T N W D D M E K I W H H T F Y N E L R V A P E E H P V L L T E A P L N P K S N R E K M T Q I M F E T F N A P A F Y V S I Q A
Full Length
21.2 kDa
1 to 140
Recombinant
6x His tag N-Terminus, Myc tag C-Terminus
Liquid
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Belongs to the actin family.
Cytoskeleton
Blue Ice
-20°C
-20°C
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
Actin also known as globular (G-actin) or filamentous (F-actin) actin plays a central role in cell structure and movement. This protein has a molecular weight of approximately 42 kDa and resides abundantly in eukaryotic cells especially in muscle and cytoskeletal structures. It comes in several isoforms with varying expression profiles across tissues. Actin can undergo polymerization from its G-actin monomers into F-actin filaments a process that is reversible through depolymerization allowing for dynamic cellular functions.
Actin contributes to various cellular processes by forming the cytoskeleton which provides mechanical support and determines cell shape. Actin also facilitates cell motility division and intracellular transport through rapid polymerization and depolymerization cycles. Within cells actin associates with other proteins to form complexes such as the Arp2/3 complex which assists actin in the branching of filaments critical for pushing forward the cell's leading edge during movement. Techniques like actin immunofluorescence help visualize actin filaments within cells revealing its extensive network.
Actin plays an integral role in pathways like cell movement and signal transduction. The Rho family of GTPases regulates actin cytoskeleton rearrangements influencing cell shape and migration. Actin function interactions involve proteins like myosin forming actomyosin complexes essential for muscle contraction and other cell motility activities. Actin polymerization and depolymerization cycles are key to the dynamic regulation within these pathways ensuring adequate cellular responses to environmental signals.
Mutations or misregulation of actin and its associated pathways link to conditions such as cardiomyopathies and cancer metastasis. In familial cardiomyopathy actin mutations disrupt normal cardiac muscle contraction. In cancer altered actin polymerization and depolymerization enable invasive cell migration facilitating metastasis. Proteins like myosin and tropomyosin associate with actin in these pathologies illustrating the impact of actin dynamics on disease progression and highlighting actin as a therapeutic target. Anti-actin antibodies can be used in research and diagnostics to better understand these disorders.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel analysis of ab235861.
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