Recombinant Human TPM3 Protein

Name: Recombinant Human TPM3 Protein
Brand: Beta LifeScience
SKU: BL-1377SG
Availability: InStock

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Product Overview

Tag	His
Host Species	Human
Accession	NM_152263
Synonym	APM1; CFTD; hscp30; NEM1; OK/SW-cl.5; TM-5; TM3; TM30; TM30nm; TM5; TPMsk3
Background	TPM3 or tropomyosin 3 is a member of the tropomyosin family of actin-binding proteins that are dimers of coiled-coil proteins that provide stability to actin filaments and regulate access of other actin-binding proteins. TPM3 involved in translocations with other loci, including anaplastic lymphoma receptor tyrosine kinase (ALK) and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which result in the formation of fusion proteins that act as oncogenes. TPM3 protein is substituted for the external domain of a putative tyrosine-kinase cell surface receptor to create the TRK oncogene (1). TPM3 are a common cause of congenital fiber type disproportion (2).
Description	Full-length recombinant human TPM3 protein was produced in E. coli, fused with a His tag at N-terminus.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	~39 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human TPM3 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subcellular Location	Cytoplasm, cytoskeleton.
Protein Families	Tropomyosin family
Database References	HGNC: 12012 OMIM: 164970 KEGG: hsa:7170 STRING: 9606.ENSP00000357516 UniGene: Hs.535581
Associated Diseases	Nemaline myopathy 1 (NEM1); Myopathy, congenital, with fiber-type disproportion (CFTD); Cap myopathy 1 (CAPM1)

Gene Functions References

Analysis of the residual, resected tumor identified a chromoplectic TPM3-ALK rearrangement that involved many other known oncogenes and was confirmed by rtPCR. PMID: 27742657
expression levels of tropomyosin 3 (TPM3) were higher in stage III ESCC tissue compared with stage I (P<0.05). The findings of the present study identified twelve proteins, which are closely associated with ESCC invasion and metastasis, apoptosis and cell signal transduction. PMID: 28138712
Dominant mutations in TPM3, encoding alpha-tropomyosinslow, cause a congenital myopathy characterized by generalized muscle weakness. Here, we used a multidisciplinary approach to investigate the mechanism of muscle dysfunction in 12 TPM3-myopathy patients. PMID: 26307083
This work expands the phenotypic spectrum of TPM3-related disease and provides insights into the pathophysiological mechanisms of the actin-tropomyosin complex PMID: 26418456
Western blot showed phosphorylation of ALK, ERK1/2, and STAT3 in cells transfected with TPM3-ALK. Coiled-coil structure of TPM3 contributes to the transforming ability of the TPM3-ALK fusion protein, and longer TPM3 region leads to higher dimer formation. PMID: 25596129
DATA show that tropomyosin 3 protein (TPM3) plays a critical role in the progression of gliomas. PMID: 24913705
study reports on a three-generation family with cap myopathy caused by a novel heterozygous mutation in TPM3 PMID: 24239060
TPM3-R167H mutations decreased cooperative thin filament activation in combination with reductions in the myosin cross-bridge number and force production. PMID: 22798622
TPM3 is an interacting partner of granulin-epithelin precursor and may play an important role in hepatocarcinogenesis. PMID: 22792281
investigation of biomarkers for early diagnosis of endometriosis: Data suggest that TPM3, stomatin-like protein 2, and tropomodulin 3 are autoantigens present in blood of women with endometriosis; immunodominant epitopes were identified. PMID: 22158085
study reports clinico-pathological and electrophysiological features of 2 unrelated cases with heterozygous TPM3 mutation; cases highlight neuromuscular transmission defect in congenital myopathy with fibre type disproportion secondary to TPM3 mutations PMID: 20951040
High TPM3-PDGFRB fusion protein expression is associated with chronic eosinophilic leukemia. PMID: 21072821
variation in the tropomyosin isoform composition of microfilaments provides a mechanism to generate functionally distinct filament populations PMID: 21036167
TPM3 mutations are involved in fiber size disproportion in congenital myotonic dystrophy PMID: 20179953
the clinical, myopathological and muscle MRI findings in a German family with autosomal dominant nemaline myopathy due to a novel pathogenic TPM3 mutation PMID: 20012312
Overexpression of TPM3 activates Snail mediated EMT, which will repress E-cadherin expression and that it confers migration or invasion potentials to HCC cells during hepatocarcinogenesis. PMID: 20356415
Conditional TPM3-ALK and NPM-ALK transgenic mice develop reversible ALK-positive early B-cell lymphoma/leukemia. PMID: 20223922
Mutations in TPM3 were identified in 6 out of 13 patients with Congenital fiber type disproportion, as well as in one case of nemaline myopathy. PMID: 19953533
cloned and sequenced a novel nonmuscle tropomyosin (hTM) isoform, TC22, which is strongly associated with colonic neoplasia and carcinoma PMID: 12105844
A mutation converting the stop codon to a serine and a second splicing mutation predicted to prevent inclusion of skeletal muscle exon IX were found associated with nemaline myopathy PMID: 12196661
De novo missense mutation in a constitutively expressed exon of the slow alpha-tropomyosin gene TPM3 associated with an atypical, sporadic case of nemaline myopathy. PMID: 12467750
tropomyosin isoforms regulate neuronal size and shape PMID: 15888546
second pedigree with autosomal dominant nemaline myopathy caused by TPM3 mutation(Arg167His). PMID: 17376686
Mutation of TPM3 is the most common cause of congenital fiber type disproportion reported to date. PMID: 18300303
The mutation reported here is the first deletion to be identified in TPM3, and it is likely to be a founder mutation in the Turkish population. PMID: 18382475
TTC9A acts as a chaperone protein to facilitate the function of tropomyosins (including Tm5NM-1) in stabilizing microfilament and it may play a role in cancer cell invasion and metastasis PMID: 18699990
We report a TPM3 mutation in one of the original cases of cap disease. PMID: 19487656

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.