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This particular function is considered a scaffold's most basic function. Scaffolds assemble signaling components of a cascade into complexes. This assembly may be able to enhance signaling specificity by preventing unnecessary interactions between signaling proteins, and enhance signaling efficiency by increasing the proximity and effective concentration of components in the scaffold complex.
Typically, phosphorylation of the C-terminal region of CAS proteins by FAK or PTK2B creates a binding site for the SH2 domain of a SRC-family protein, which then hyper-phosphorylates the substrate domain, allowing the CAS protein to function as a scaffold [30] for other proteins including CRK proteins and C3G, a guanine nucleotide exchange ...
These proteins differ in activity and subcellular locations, p66 is the longest and while the p52 and p46 link activated receptor tyrosine kinase to the RAS pathway. [6] The protein SHC1 also acts as a scaffold protein which is used in cell surface receptors. [7] The three proteins that SHC1 codes for have distinctly different molecular weights ...
the description of scaffold-attachment elements (SARs) by Laemmli and coworkers, which were thought to demarcate the borders of a given chromatin domain [2] the characterization of matrix-associated regions (MARs) the first examples of which supported the immunoglobulin kapp-chain enhancer according to its occupancy with transcription factors [ 3 ]
Discs large homolog 1 (DLG1), also known as synapse-associated protein 97 or SAP97, is a scaffold protein that in humans is encoded by the SAP97 gene. SAP97 is a mammalian MAGUK -family member protein that is similar to the Drosophila protein Dlg1 (the protein is alternatively referred to as hDlg1, and the human gene is DLG1).
Although several protein families have four transmembrane alpha-helices, tetraspanins are defined by conserved amino acid sequences including four or more cysteine residues in the EC2 domain, with two in a highly conserved 'CCG' motif. Tetraspanins are often thought to act as scaffolding proteins, anchoring multiple proteins to one area of the ...
The septins act as a scaffold, recruiting many proteins. These protein complexes are involved in cytokinesis, chitin deposition, cell polarity, spore formation, in the morphogenesis checkpoint, spindle alignment checkpoint and bud site selection.
Annexins can function as scaffolding proteins to anchor other proteins to the cell membrane. Annexins assemble as trimers, [8] where this trimer formation is facilitated by calcium influx and efficient membrane binding. This trimer assembly is often stabilized by other membrane-bound annexin cores in the vicinity.
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