TPM2
TPM2 (tropomyosin 2) encodes beta-tropomyosin, an actin filament-binding protein of the tropomyosin family that is found in muscle and non-muscle cells. It is also known as DA1, NEM4 and AMCD1, and it helps regulate striated muscle contraction. Browse Assay Genie's current range of TPM2 research reagents below, or read on for the biology behind the target.
TPM2 binds to actin filaments in both muscle and non-muscle cells. In association with the troponin complex, it plays a central role in the calcium-dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is instead regulated through interaction with caldesmon. In non-muscle cells, tropomyosin is implicated in stabilising cytoskeletal actin filaments, and the non-muscle isoform may have a role in agonist-mediated receptor internalisation.
The TPM2 gene encodes beta-tropomyosin, a member of the actin filament binding protein family that belongs to the tropomyosin gene group. The protein is mainly expressed in slow, type 1 muscle fibres. Alternatively spliced transcript variants encode different isoforms, which fits the distinct muscle and non-muscle roles described for the protein. The mouse and rat orthologues are both named Tpm2.
Mutations in the TPM2 gene can alter the expression of other sarcomeric tropomyosin proteins. They cause cap disease, nemaline myopathy and distal arthrogryposis syndromes. This is reflected in the gene's aliases and earlier names, including DA1, NEM4, AMCD1, "arthrogryposis multiplex congenital, distal, type 1" and "tropomyosin 2 (beta)". TPM2 is therefore a useful target for work on sarcomere function, actin cytoskeleton regulation and inherited muscle disease.
TPM2 works with the troponin complex in the calcium-dependent regulation of striated muscle contraction.
TPM2 mutations cause cap disease, nemaline myopathy and distal arthrogryposis syndromes, so the gene is relevant to muscle disease studies.
In non-muscle cells, tropomyosin is implicated in stabilising actin filaments of the cytoskeleton.
Beta-tropomyosin is mainly expressed in slow, type 1 muscle fibres, making TPM2 relevant to fibre-type characterisation.
TPM2 binds actin filaments in muscle and non-muscle cells. With the troponin complex it regulates calcium-dependent striated muscle contraction, and in non-muscle cells it helps stabilise actin filaments. The non-muscle isoform may also contribute to agonist-mediated receptor internalisation.
TPM2 is also called DA1, NEM4 and AMCD1, and was previously named tropomyosin 2 (beta). UniProt lists the product as tropomyosin beta chain. Alternatively spliced transcript variants encode different isoforms, including a non-muscle isoform.
Yes. Mutations in the TPM2 gene cause cap disease, nemaline myopathy and distal arthrogryposis syndromes. Orthologues named Tpm2 exist in mouse and rat; check the datasheet of any product for its validated reactivity.
Other tropomyosin family members and related targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P07951; product specifications from Assay Genie datasheets.