Recombinant Human Tropomyosin beta chain (TPM2), partial

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Code CSB-EP024105HU1
MSDS
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
TMSB
Uniprot No.
Research Area
Signal Transduction
Alternative Names
Alpha tropomyosin; AMCD1; Arthrogryposis multiplex congenital distal type 1; Beta tropomyosin; Beta-tropomyosin; Cytoskeletal tropomyosin TM30; DA1; DA2B; epididymis secretory protein Li 273; FLJ41118; Heat stable cytoskeletal protein 30 kDa; HEL-S-273; hscp30; HTM alpha; hTM5; MGC14582; MGC3261; MGC72094; NEM1; NEM4; Nemaline myopathy type 4; OK/SW cl.5; Sarcomeric tropomyosin kappa; TM 5; TM3; TM30; TM30nm; TMSA; TMSB; TPM 1; TPM 3; TPM1 alpha; TPM1 kappa; TPM2; TPM2_HUMAN; TRK; Tropomyosin 1 alpha; Tropomyosin 1 alpha chain; Tropomyosin 1 alpha chain isoform 6; Tropomyosin 2 (beta); Tropomyosin 2; Tropomyosin 3; Tropomyosin alpha 3 chain; Tropomyosin alpha striated muscle isoform; Tropomyosin beta chain; Tropomyosin gamma; Tropomyosin skeletal muscle beta; Tropomyosin-2
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
14-284aa
Target Protein Sequence
DKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
35.3kDa
Protein Length
Partial
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

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. The non-muscle isoform may have a role in agonist-mediated receptor internalization.
Gene References into Functions
  1. Hypoxia may regulate cell invasiveness partly by TPM2 down-regulation mediated changes of MMP2 expression, which is also a new pathway by which hypoxia regulates cancer progression. TPM2 is a potential novel tumour suppressor gene in breast cancer. PMID: 29414807
  2. The increased expression of TPM1lambda and the decreased expression of TPM1delta RNA and TPM2beta may lead to decreased stress fiber formation and malignant transformation in human breast epithelial cells. PMID: 27108600
  3. TPM2 appears to be commonly silenced by aberrant DNA methylation in colon cancer. TPM2 loss is associated with RhoA activation and tumor proliferation. PMID: 27333992
  4. Despite its reduced affinity for actin in co-sedimentation assay, the Q147P mutant incorporates into the muscle fiber ..Q147P tropomyosin (TPM2)binds to actin in ghost muscle fiber. PMID: 26708479
  5. tropomyosin 2.1 acts as a suppressor of growth on soft matrices by supporting proper rigidity sensing PMID: 26619148
  6. Myo1c significantly increases the frequency of kinesin-1-driven microtubule-based runs that begin at actin/microtubule intersections. The actin-binding protein tropomyosin 2 abolishes Myo1c-specific effects on both run initiation and run termination. PMID: 25660542
  7. Patients with TPM2 mutations tended to present with milder symptoms than those with TPM3 mutations, DA being present only in the TPM2 group. PMID: 24692096
  8. in a cohort of 94 patients with congenital myopathy, 2 related female patients and 2 sporadic male patients were found to carry mutations in TPM2 and TPM3 genes respectively; clinical presentation and muscle morphological findings differed in the patients PMID: 24507666
  9. Histopathological phenotype association of muscle fibers expressing Beta-tropomyosin mutational variants that occur in human myopathies. PMID: 24039757
  10. effect of the skeletal myopathy-causing E117K mutation in human beta-tropomyosin on actomyosin structure during the ATPase cycle PMID: 24657080
  11. We showed that TPM2, CLU, and COL4A6 mRNA levels are downregulated in prostate cancer. PMID: 23621580
  12. The p.R133W mutation in TPM2 is associated with Sheldon-Hall syndrome. PMID: 23678273
  13. The E117K mutation in tropomyosin beta chain that causes nemaline myopathy shifts the tropomyosin strands to the closed position and suppresses their conformational rearrangements on the thin filament. PMID: 23689010
  14. expanding the spectrum of TPM2 myopathies to very mild patients who could still be pathologically recognized by the presence of cap structures PMID: 23015096
  15. Novel de novo missense mutations in TPM2 were found to be associated with marked fibre size disproportion in two patients with congenital fibre type disproportion. PMID: 22832343
  16. The TPM2-null mutations decreased cooperative thin filament activation in combination with reductions in the myosin cross-bridge number and force production PMID: 22798622
  17. distal arthrogryposis syndromes associated with TPM2 mutations include the less severe forms[review] PMID: 22749895
  18. A novel beta-tropomyosin mutation is described that is associated with two clinical-histopathological phenotypes not previously associated with it. PMID: 23413262
  19. p.K7del is a common hetreozygous recurrent TPM2 mutation associated with nemaline myopathy. PMID: 23378224
  20. This study demonistrated that most patients with TPM2 mutations show a predominant involvement of masticatory and distal leg muscles with the other regions relatively spared. PMID: 22980765
  21. actin binding was weak in three of five mutants suggesting that abnormal binding between actin and aberrant Tm is the pathogenetic mechanism causing muscle weakness in patients with nemaline and cap myopathy. PMID: 22084935
  22. in cells expressing R133W beta-tropomyosin mutation, during activation, switching of positive to neutral charge at position 133 partially hinders calcium- and myosin-induced tropomyosin movement over the thin filament blocking actin conformation change PMID: 20457903
  23. While demonstrating suppressed levels of Tm1 in the prostate cancer cell lines LNCaP, PC3, and DU-145 compared to normal prostate epithelial cell primary isolates, a novel splice variant of the TPM2 gene was identified. PMID: 20336778
  24. Tropomyosin 2 plays a role in growth and metastasis of hepatic tumors. PMID: 18246790
  25. beta-tropomyosin exon 6B splicing requires hnRNP A1 and ASF/SF2 and SC35 PMID: 15208309
  26. We describe two patients, a woman and her daughter, with muscle weakness and distal arthrogryposis (DA) type 2B, caused by a heterozygous missense mutation, R133W. PMID: 17339586
  27. R133W beta-Tm mutation induces alterations in myosin-actin kinetics causing a reduced number of myosin molecules in the strong actin-binding state, resulting in overall muscle weakness in the absence of muscle wasting. PMID: 17430991
  28. results indicate that mutations in TPM2 may cause nemaline myopathy as well as cap disease with a dominant mode of inheritance; these disorders may thus be phenotypic variants of the same genetic defect PMID: 17846275
  29. beta-TM gene mutations can alter the expression of other sarcomeric TM isoforms PMID: 18422639
  30. Mutations in TPM2 seem to be a frequent cause of cap disease. PMID: 19047562
  31. This first report of the clinical expression of the complete absence of TPM2 in human indicated that TPM2 expression at the early period of prenatal life plays a major role for normal fetal movements. PMID: 19155175
  32. The destabilizing effect of the disease-causing arginine91glycine mutation spreads along the coiled-coil, reflecting the high extent of cooperativity within this part of the beta-tropomyosin molecule. [review] PMID: 19214762
  33. Our patient has an identical TPM2 mutation to the first genetically diagnosed cap disease patient, a denovo heterozygous three base pair deletion that removes glutamic acid 139 from the centre of beta-tropomyosin. PMID: 19345583

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Involvement in disease
Nemaline myopathy 4 (NEM4); Arthrogryposis, distal, 1A (DA1A); Cap myopathy 2 (CAPM2); Arthrogryposis, distal, 2B (DA2B)
Subcellular Location
Cytoplasm, cytoskeleton.
Protein Families
Tropomyosin family
Tissue Specificity
Present in primary breast cancer tissue, absent from normal breast tissue.
Database Links

HGNC: 12011

OMIM: 108120

KEGG: hsa:7169

STRING: 9606.ENSP00000354219

UniGene: Hs.300772

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