Recombinant Human Tropomyosin Alpha-3 Chain (TPM3) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03966P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Tropomyosin Alpha-3 Chain (TPM3) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03966P
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Product Overview

Description Recombinant Human Tropomyosin Alpha-3 Chain (TPM3) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P06753
Target Symbol TPM3
Synonyms Alpha tropomyosin 3; Alpha tropomyosin slow skeletal; CFTD; Cytoskeletal tropomyosin TM30; FLJ41118; gamma TM; Gamma tropomyosin; Gamma-tropomyosin; Heat stable cytoskeletal protein 30 kDa; hscp30; hTM30nm; hTM5; hTMnm; MGC102590; MGC14582; MGC3261; MGC72094; NEM1; OK/SW-cl.5; OTTHUMP00000034019; OTTHUMP00000034171; OTTHUMP00000034172; TM 5; TM-5; TM3; TM30; TM30nm; TM5; Tm5NM; Tpm 5; TPM3; TPM3/NTRK1 FUSION GENE, INCLUDED; TPM3_HUMAN; Tpm5; TPMsk3; TRK; TRK ONCOGENE, INCLUDED; Trop 5; Tropomyosin 3; Tropomyosin 3 gamma; Tropomyosin 5; Tropomyosin alpha 3 chain; Tropomyosin alpha-3 chain; Tropomyosin gamma; Tropomyosin-3; Tropomyosin-5
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Expression Range 2-285aa
Protein Length Full Length of Mature Protein
Mol. Weight 59.8kDa
Research Area Signal Transduction
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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

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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.

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