Product Description
Size: 100µg
Anti-TAGLN/Transgelin antibody (ab10135) is a goat polyclonal antibody detecting TAGLN/Transgelin in Western Blot, Flow Cytometry, IHC-P, IHC-Fr, ICC/IF . Suitable for Human, Mouse, Rabbit, Rat . - Over 130 publications - Trusted since 2004
Key facts
Host species:Goat,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Human, Rat, Mouse, Rabbit,
Applications:WB, ICC/IF, IHC-P, Flow Cyt, IHC-FoFr, IHC-FrSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human TAGLN aa 150-200. The exact immunogen used to generate this antibody is proprietary information.Q01995
Product details:
What is this antibody validated in?
Anti-TAGLN/Transgelin antibody (ab10135) is a goat polyclonal antibody and is validated for use in Western Blot (WB), Flow Cytometry (Flow Cyt), Immunohistochemistry (IHC-P), Immunohistochemistry (IHC-Fr), Immunocytochemistry/immunofluorescence (ICC/IF) in Human, Mouse, Rabbit, Rat samples.
Tagged protein detection
TAGLN/Transgelin antibodies are used to visualize proteins labelled with this tag in a variety of applications.
What is the molecular weight of TAGLN/Transgelin?
Anti-TAGLN/Transgelin (ab10135) specifically detects a band for TAGLN/Transgelin (UniProt: Q01995) at a molecular weight of 23kDa.
Trusted by the scientific community
Anti-TAGLN/Transgelin (ab10135) was first used in a scientific publication in 2004 and has been cited over 130 times in peer-reviewed journals.
Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Purification notes-Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide., Storage buffer-pH: 7.3Preservative: 0.02% Sodium azideConstituents: Tris buffered saline, 0.5% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
TAGLN also known as Transgelin or SM22-alpha is a protein with a molecular weight of approximately 22 kDa. Structurally it belongs to the calponin family and contains an ACT domain which is critical for its actin-binding ability. It is expressed abundantly in smooth muscle cells where it stabilizes cytoskeletal dynamics by interacting with actin filaments. TAGLN also shows expression in fibroblasts and myofibroblasts supporting structural integrity and cellular movement.
Biological function summary
The regulatory involvement of TAGLN in smooth muscle contraction influences cellular activities essential for vascular function. This protein modulates remodeling and differentiation within smooth muscle cells. It can associate with actin and calponin to form complexes that regulate the stability of cytoskeletal structures ensuring effective cellular responses to mechanical stimuli. By linking signal transduction to cytoskeletal mechanics TAGLN facilitates the maintenance of cell shape and tension.
Pathways
TAGLN plays a role in the regulation of the RhoA/Rho kinase pathway contributing to actin cytoskeleton organization and smooth muscle contraction. Additionally it is involved in the WNT signaling pathway influencing cell proliferation and differentiation. In these pathways TAGLN works with proteins like RhoA and beta-catenin to transmit signals from the extracellular environment to the nucleus impacting gene expression and cellular responses.
Disruptions in TAGLN expression associate with vascular diseases and certain cancers. Downregulation or altered expression patterns can lead to smooth muscle cell dysfunction contributing to atherosclerosis. Similarly TAGLN interacts with proteins such as fibronectin and MMP2 in cancer where its altered expression could promote metastasis and tumor progression. Understanding these connections highlights TAGLN's potential as a target for therapeutic interventions in these diseases.
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Collaboration
Tony Tang
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