Tropomyosin beta chain Recombinant Protein | TMSB recombinant protein

Recombinant Human Tropomyosin beta chain

Cat. Num. AAA954251

• Gene Names: TPM2; DA1; DA2B; NEM4; TMSB; AMCD1; HEL-S-273
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Tropomyosin beta chain; Recombinant Human Tropomyosin beta chain; Beta-tropomyosin; Tropomyosin-2; TMSB recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 14-284aa; Partial
• Sequence: DKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
• Sequence Length: 284

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for TMSB recombinant protein

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.

Product Categories/Family for TMSB recombinant protein

Signal Transduction

References

A muscle-type tropomyosin in human fibroblasts evidence for expression by an alternative RNA splicing mechanism.MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K., Modi G., Walsh F.S.Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985) Complete nucleotide sequence of the adult skeletal isoform of human skeletal muscle beta-tropomyosin.Widada J.S., Ferraz C., Capony J.-P., Liautard J.-P.Nucleic Acids Res. 16:3109-3109(1988) A cDNA encoding a muscle-type tropomyosin cloned from a human epithelial cell line identity with human fibroblast tropomyosin TM1.Prasad G.L., Meissner S., Sheer D.G., Cooper H.L.Biochem. Biophys. Res. Commun. 177:1068-1075(1991) Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004)

NCBI and Uniprot Product Information

• NCBI GI #: 42476296
• NCBI GeneID: 7169
• NCBI Accession #: NP_003280.2
• NCBI GenBank Nucleotide #: NM_003289.3
• UniProt Accession #: P07951; P06468; Q13894; Q53FM4; Q5TCU4; Q5TCU7; Q9UH67; A6NM85
• Molecular Weight: 35.3 kDa
• NCBI Official Full Name: tropomyosin beta chain isoform Tpm2.2st
• NCBI Official Synonym Full Names: tropomyosin 2 (beta)
• NCBI Official Symbol: TPM2
• NCBI Official Synonym Symbols: DA1; DA2B; NEM4; TMSB; AMCD1; HEL-S-273
• NCBI Protein Information: tropomyosin beta chain
• UniProt Protein Name: Tropomyosin beta chain
• Protein Family: Thymosin
• UniProt Gene Name: TPM2
• UniProt Synonym Gene Names: TMSB
• UniProt Entry Name: TPM2_HUMAN

NCBI Description

This gene encodes beta-tropomyosin, a member of the actin filament binding protein family, and mainly expressed in slow, type 1 muscle fibers. Mutations in this gene can alter the expression of other sarcomeric tropomyosin proteins, and cause cap disease, nemaline myopathy and distal arthrogryposis syndromes. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Mar 2009]

Uniprot Description

TPM2: 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. Defects in TPM2 are the cause of nemaline myopathy type 4 (NEM4). A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-or rod-like structures in muscle fibers on histologic examination. Nemaline myopathy type 4 presents from infancy to childhood with hypotonia and moderate-to-severe proximal weakness with minimal or no progression. Major motor milestones are delayed but independent ambulation is usually achieved, although a wheelchair may be needed in later life. Defects in TPM2 are the cause of distal arthrogryposis type 1A (DA1A). A form of distal arthrogryposis, a disease characterized by congenital joint flexures or contractures that mainly involve the distal parts of the limbs, and affect two or more different body areas in the absence of a primary neurological or muscle disease. Distal arthrogryposis type 1 is characterized largely by camptodactyly and clubfoot. Hypoplasia and/or absence of some interphalangeal creases is common. The shoulders and hips are less frequently affected. Belongs to the tropomyosin family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Motor; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 9p13

Cellular Component: cytosol; muscle thin filament tropomyosin

Molecular Function: actin binding; structural constituent of muscle

Biological Process: muscle contraction; muscle filament sliding; regulation of ATPase activity

Disease: Arthrogryposis, Distal, Type 1a; Arthrogryposis, Distal, Type 2b; Myopathy, Congenital, With Fiber-type Disproportion; Nemaline Myopathy 4