Recombinant Human Tropomyosin Beta Chain (TMSB) Protein (His)

Name: Recombinant Human Tropomyosin Beta Chain (TMSB) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03558P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Tropomyosin Beta Chain (TMSB) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07951
Target Symbol	TMSB
Synonyms	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)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
Expression Range	14-284aa
Protein Length	Partial
Mol. Weight	35.3kDa
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. The non-muscle isoform may have a role in agonist-mediated receptor internalization.
Subcellular Location	Cytoplasm, cytoskeleton.
Protein Families	Tropomyosin family
Database References	HGNC: 12011 OMIM: 108120 KEGG: hsa:7169 STRING: 9606.ENSP00000354219 UniGene: PMID: 29414807 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 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 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 tropomyosin 2.1 acts as a suppressor of growth on soft matrices by supporting proper rigidity sensing PMID: 26619148 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 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 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 Histopathological phenotype association of muscle fibers expressing Beta-tropomyosin mutational variants that occur in human myopathies. PMID: 24039757 effect of the skeletal myopathy-causing E117K mutation in human beta-tropomyosin on actomyosin structure during the ATPase cycle PMID: 24657080 We showed that TPM2, CLU, and COL4A6 mRNA levels are downregulated in prostate cancer. PMID: 23621580 The p.R133W mutation in TPM2 is associated with Sheldon-Hall syndrome. PMID: 23678273 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 expanding the spectrum of TPM2 myopathies to very mild patients who could still be pathologically recognized by the presence of cap structures PMID: 23015096 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 The TPM2-null mutations decreased cooperative thin filament activation in combination with reductions in the myosin cross-bridge number and force production PMID: 22798622 distal arthrogryposis syndromes associated with TPM2 mutations include the less severe forms[review] PMID: 22749895 A novel beta-tropomyosin mutation is described that is associated with two clinical-histopathological phenotypes not previously associated with it. PMID: 23413262 p.K7del is a common hetreozygous recurrent TPM2 mutation associated with nemaline myopathy. PMID: 23378224 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 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 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 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 Tropomyosin 2 plays a role in growth and metastasis of hepatic tumors. PMID: 18246790 beta-tropomyosin exon 6B splicing requires hnRNP A1 and ASF/SF2 and SC35 PMID: 15208309 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 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 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 beta-TM gene mutations can alter the expression of other sarcomeric TM isoforms PMID: 18422639 Mutations in TPM2 seem to be a frequent cause of cap disease. PMID: 19047562 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 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 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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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.