src

pp60 c-src (521-533) (phosphorylated) acetate is a regulator of focal adhesion formation and cell spreading. pp60 c-src (521-533) (phosphorylated) acetate also regulates cell motility and is a key component in the signaling pathway triggered by the motogenic hyaluronan receptor RHAMM.

RR-src acetate is a synthetic peptide derived from the amino acid sequence surrounding the phosphorylation site in pp60src.

SRC-1 (686-700) is a bioactive peptide encompassing amino acids 686 to 700, which include the second LXXLL motif from NR box II of steroid receptor coactivator (SRC1). These coactivator proteins facilitate transcription by ligand-dependent interaction with nuclear receptors.

P60v-src(137-157) is a synthetic peptide that serves as an inhibitor of the tyrosine kinase activity of p60 v-src, with an IC50 value of 7.5 μM [1] [2].

Peptide corresponding to the pp60c-src carboxy terminal regulatory domain; phosphorylated at Tyr527. Binds to pp60c-src and pp60v-src at the SH2 domain, suppressing their tyrosine kinase activity and transforming potential.

Phosphorylated p60c-src substrate II is a pentapeptide and a phosphorylated polypeptide form of p60c-src substrate II. Phosphorylation is a critical post-translational modification (post-translationmodification) vital for biological regulatory processes [1].

pp60 (v-SRC) Autophosphorylation Site, Phosphorylated is a phosphorylated peptide derived from an EGFR substrate. It serves as a valuable tool for quantifying phosphorylated substrates in screening EGFR Kinase inhibitors.

Tyrosine kinase substrate peptide

P60c-src substrate II is a potent pentapeptide substrate for the tyrosine kinase pp60c-src [1].

Src Optimal Peptide Substrate, a highly specific substrate of Src, serves as a reliable indicator of Src activity. It enables accurate assessment of Src kinase function.

Osteogenic Growth Peptide (10-14) acetate (Osteogenic Growth Peptide) is a Src inhibitor and an effective mitogen and stimulator of osteogenesis and hematopoiesis. Osteogenic Growth Peptide (10-14) acetate is responsible for the binding to the OGP receptor and activates an intracell

EPQpYEEIPIYL, a phosphopeptide, is a ligand for the Src homology 2 (SH2) domain. It activates members of the Src family, such as Lck, Hck, and Fyn, through the binding interaction with SH2 domains.

Phosphopeptide ligand for the src SH2 domain (IC50 = 42 nM); displays 30-fold higher affinity than N-acetyl-O-phosphono-Tyr-Glu-Glu-Ile-Glu (Ac-pYEEIE,).

Secretin is an endocrine hormone that stimulates the secretion of bicarbonate-rich pancreatic fluids. Canine secretin can regulates gastric chief cell function and paracellular permeability in canine gastric monolayers by a Src kinase-dependent pathway.

Phosphopeptide ligand for the src SH2 domain (IC50 = 1 μM). Blocks src interactions with EGFR and FAK.

Ac-Tyr(PO3H2)-Glu-Glu-Ile-Glu-OH TFA (compound 1) serves as a high-affinity pentapeptide that binds to the src SH2 domain with an IC 50 value of approximately 1 µM. Additionally, it acts as an inhibitor of src SH3-SH2: phosphoprotein interactions [1].

Phosphopeptide; binds to the src SH2 domain.

Tyrosine Kinase Peptide 1 is a control substrate peptide for c-Src assay.

ND1-YL2 is a peptide-based PROTAC®Degrader of steroid receptor co-activator 1 (SRC-1; also known as nuclear receptor coactivator 1, NCOA1). ND1-YL2 is composed of a stapled peptide that binds SRC-1 (YL2) joined by a linker to a tetrapeptide that binds UBR box domains. Upon ternary complex formation, SRC-1 is polyubiquitinated and subsequently degraded via the N-degron pathway. This Degrader induces dose-dependent degradation of SRC-1 in the MDA-MB-231 triple negative breast cancer cell line (DC50 = 10 μM), and binds to the PAS-B domain of SRC-1 (Ki = 320 nM). ND1-YL2 inhibits MDA-MB-231 cell migrationin vitro, and suppresses metastasis of MDA-MB-231 cellsin vivo.