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The region for expressing recombinant Human TLN1 contains amino acids 92-399. The theoretical molecular weight of the TLN1 protein is 62.8 kDa. This protein is generated in a e.coli-based system. The N-terminal GST tag was fused into the coding gene segment of TLN1, making it easier to detect and purify the TLN1 recombinant protein in the later stages of expression and purification.The human talin-1 (TLN1) is a cytoskeletal protein that plays a crucial role in cell adhesion by connecting integrin receptors to the actin cytoskeleton. TLN1 is essential for the formation and stabilization of focal adhesions, dynamic structures that mediate cell-extracellular matrix interactions. Through its interactions with integrins, TLN1 contributes to processes such as cell migration, spreading, and signaling. Additionally, TLN1 is involved in mechanotransduction, transmitting mechanical forces across the cell membrane. Dysregulation of TLN1 has been linked to various diseases, including cancer and cardiovascular disorders. Research on TLN1 explores its functions in cell adhesion, and signaling, and its implications in health and disease.
The region for expressing recombinant Human TLN1 contains amino acids 92-399. The theoretical molecular weight of the TLN1 protein is 62.8 kDa. This protein is generated in a e.coli-based system. The N-terminal GST tag was fused into the coding gene segment of TLN1, making it easier to detect and purify the TLN1 recombinant protein in the later stages of expression and purification.The human talin-1 (TLN1) is a cytoskeletal protein that plays a crucial role in cell adhesion by connecting integrin receptors to the actin cytoskeleton. TLN1 is essential for the formation and stabilization of focal adhesions, dynamic structures that mediate cell-extracellular matrix interactions. Through its interactions with integrins, TLN1 contributes to processes such as cell migration, spreading, and signaling. Additionally, TLN1 is involved in mechanotransduction, transmitting mechanical forces across the cell membrane. Dysregulation of TLN1 has been linked to various diseases, including cancer and cardiovascular disorders. Research on TLN1 explores its functions in cell adhesion, and signaling, and its implications in health and disease.
| Cat.No | ACP02779 | Target Name | TLN1 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 92-399aa | Mol Weight | 62.8 kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q9Y490 |
|---|
Uniprot Id
Q9Y490
Target Species
Human
Target Name
TLN1
Target Full Name
Talin-1
Target Function
Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
Target Subcellular Location
Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell surface. Cell junction, focal adhesion.
Target Research Area
Signal Transduction
Target Synonyms
ILWEQ; Talin 1; Talin; Talin-1; TLN 1; TLN; Tln1; TLN1_HUMAN
Target Background
This gene encodes a cytoskeletal protein that is concentrated in areas of cell-substratum and cell-cell contacts. The encoded protein plays a significant role in the assembly of actin filaments and in spreading and migration of various cell types, including fibroblasts and osteoclasts. It codistributes with integrins in the cell surface membrane in order to assist in the attachment of adherent cells to extracellular matrices and of lymphocytes to other cells. The N-terminus of this protein contains elements for localization to cell-extracellular matrix junctions. The C-terminus contains binding sites for proteins such as beta-1-integrin, actin, and vinculin.
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