Titin (TTN), partial, human, recombinant

Titin (TTN), partial, human, recombinant
Item number Size Datasheet Manual SDS Delivery time Quantity Price
CSB-EP025267HU.20 20 µg -

10 - 14 business days*

247.00€
CSB-EP025267HU.100 100 µg -

10 - 14 business days*

446.00€
CSB-EP025267HU.1 1 mg -

10 - 14 business days*

1,850.00€
 
Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 14257-14543aa. Protein Length:... more
Product information "Titin (TTN), partial, human, recombinant"
Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 14257-14543aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: RCEEGKDNWI RCNMKLVPEL TYKVTGLEKG NKYLYRVSAE NKAGVSDPSE ILGPLTADDA FVEPTMDLSA FKDGLEVIVP NPITILVPST GYPRPTATWC FGDKVLETGD RVKMKTLSAY AELVISPSER SDKGIYTLKL ENRVKTISGE IDVNVIARPS APKELKFGDI TKDSVHLTWE PPDDDGGSPL TGYVVEKREV SRKTWTKVMD FVTDLEFTVP DLVQGKEYLF KVCARNKCGP GEPAYVDEPV NMSTPATVPD PPENVKWRDR TANSIFLTWD PPKNDGG. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. 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. Storage: 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. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase. Reference: "Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity." Freiburg A., Trombitas K., Hell W., Cazorla O., Fougerousse F., Centner T., Kolmerer B., Witt C., Beckmann J.S., Gregorio C.C., Granzier H., Labeit S. Circ. Res. 86:1114-1121(2000). Function: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.
Keywords: TTN, Titin, Connectin, EC=2.7.11.1, Rhabdomyosarcoma antigen MU-RMS-40.14, Recombinant Human Titin (TTN), partial
Supplier: Cusabio
Supplier-Nr: EP025267HU

Properties

Application: Activity not tested
Conjugate: No
Host: E.coli
Species reactivity: human
MW: 36.9 kD
Purity: >85% (SDS-PAGE)

Handling & Safety

Storage: -20°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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