protein kinase c β pseudosubstrate

PKC β pseudosubstrate acetate (PKC β pseudosubstrate acetate (172308-76-8 Free base)) is a selective cell-permeable inhibitor of PKC.

Protein Kinase C 19-31 acetate, a peptide inhibitor of protein kinase C (PKC), derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as protein kinase C substrate

Protein Kinase C Peptide Substrate acetate targets specific cell spacers ina manner that is dependent on second messengers and specific adaptor proteins in response to extracellular signals that activate g protein-coupled receptors, tyrosine Kinase recept

Activated Protein C (390-404), human acetate (Activated Protein C ) inhibits APC anticoagulant activity.

C-Reactive Protein (CRP) 201-206 acetate (C-Reactive Protein ) is the 201-206 fragment of C-Reactive Protein. C-Reactive Protein (CRP) acetate, the prototypic marker of inflammation, is a cardiovascular risk marker and may promote atherogenesis.

C-Reactive Protein (CRP) 77-82 acetate is the 77-82 fragment of C-Reactive Protein. C-Reactive Protein (CRP), the prototypic marker of inflammation, is a cardiovascular risk marker and may promote atherogenesis.C-reactive protein (CRP) is an annular (ring

Calmodulin-Dependent Protein Kinase II 290-309 acetate is an effective antagonist of Ca2+/calmodulin-dependent protein kinase II (IC50 = 52 nM).

C-Reactive Protein (CRP) 174-185 acetate is an acute phase serum protein synthesized in response to inflammatory cytokines, produces antitumor effects in animals. The fragment CRP (174-185) (RS-83277) shows similar activity by significantly enhancing the

Protein Kinase C (661-671), a fragment peptide of the β1 subspecies of Protein Kinase C (PKC), is instrumental in regulating cellular growth and has been implicated in tumor promotion [1] [2].

Protein Kinase C βII V5 peptide (660-673) (PKC βII (660-673)) exhibits an affinity for binding to RACK1 [1].

Calmodulin Dependent Protein Kinase Substrate is a synthetic peptide that interacts specifically with calmodulin-dependent protein kinases (CaMK) and requires calcium ions (Ca 2+) and calmodulin (CaM) for activation. It is utilized in studies involving protein kinase activity [1].

CRP, an acute phase serum protein synthesized in response to inflammatory cytokines, produces antitumor effects in animals. The fragment CRP (174-185) (RS-83277) shows similar activity by significantly enhancing the tumoricidal activity of human monocytes

Protein Kinase C Peptide Substrate targets specific cell spacers ina manner that is dependent on second messengers and specific adaptor proteins in response to extracellular signals that activate g protein-coupled receptors, tyrosine Kinase receptors, or

Calmodulin-Dependent Protein Kinase II (290-309) acetate is a potent CaMK antagonist with an IC50 of 52 nM for the inhibition of Ca2+ calmodulin-dependent protein kinase II [1].

Protein Kinase C (gamma) Peptide, a fragment of Protein Kinase Cγ, plays a role in dominant ataxia by inhibiting the nuclear import of aprataxin, which is associated with recessive ataxia [1].

EGFR Protein Tyrosine Kinase Substrate is an EGFR protein tyrosine kinase substrate.

Protein Kinase C (19-31), a peptide inhibitor derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as a substrate peptide for testing protein kinase C activity.

Protein Kinase C (19-35) Peptide, acting as a PKC pseudosubstrate inhibitor region, can potentially inhibit PKC activity by blocking the substrate-binding site within the kinase domain, thereby inactivating the cytoplasmic form of PKC [1] [2].

Protein Kinase C (alpha) Peptide (TFA) is a PKC-α-associated peptide functioning as a lipid-dependent serine/threonine protein kinase. It plays a pivotal role in regulating several cellular functions such as survival, proliferation, differentiation, migration, and adhesion [1].

Protein Kinase C (19-36) is a pseudosubstrate peptide that inhibits protein kinase C (PKC) with an IC50 of 0.18 μM.

Activated Protein C (390-404), human, a peptide derived from the vitamin K-dependent serine protease, effectively suppresses the anticoagulant activity of APC [1].

Calmodulin-Dependent Protein Kinase II (290-309) is a potent CaMK antagonist with an IC50 of 52 nM for inhibiting Ca2+ calmodulin-dependent protein kinase II.

Protein kinase inhibitor peptide matches the inhibitory domain of the heat-stable protein kinase inhibitor.

C-Reactive Protein (CRP) 77-82 is the 77-82 fragment of C-Reactive Protein. CRP, the prototypic marker of inflammation, is a cardiovascular risk marker and may promote atherogenesis. CRP is an annular (ring-shaped), pentameric protein found in blood plasma, whose circulating concentrations rise in response to inflammation. It is an acute-phase protein of hepatic origin that increases following interleukin-6 secretion by macrophages and T cells.

Protein Kinase C (19-31) TFA is a peptide inhibitor derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31), featuring a serine substitution for alanine at position 25. It serves as a substrate peptide for evaluating Protein Kinase C (PKC) activity, playing a crucial role in modulating protein functions by phosphorylating the hydroxyl groups of serine and threonine amino acids on target proteins [1] [2].

Calmodulin-Dependent Protein Kinase II (281-309) is a synthetic peptide phosphorylatable at Thr286 by PKC, inhibiting CaM kinase II with an IC50 of 80 nM.

C-Reactive Protein (CRP) Fragment (201-206) is a peptide segment derived from C-Reactive Protein (CRP), the quintessential indicator of inflammation. As a cardiovascular risk marker, CRP may facilitate atherogenesis.

Protein Kinase C (beta) Peptide, a fragment of Protein Kinase Cβ, is associated with hyperglycemia-induced decreases in endothelium-derived nitric oxide. Inhibiting Protein Kinase Cβ forestalls the impairment of endothelium-dependent vasodilation caused by acute hyperglycemia [1].

Protein Kinase C substrate, a specific substrate of Protein Kinase C, plays a pivotal role in signal transduction by facilitating the detection of protein through its enzyme's catalytic action on specific substrate phosphorylation [1].

Calmodulin-Dependent Protein Kinase Substrate Analog, a synthetic peptide substrate, is activated by Ca2+ and calmodulin (CaM). It serves as a substrate for protein kinases, leveraging a dependency on Ca2+ and CaM for its function [1].

Protein Kinase C (19-31) TFA, a peptide inhibitor of protein kinase C (PKC), derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as protein kinase C substrate p

Tyrosine Protein Kinase JAK 2 (Phospho-Tyr8, 9) is a peptide derived from mouse JAK2, consisting of amino acids 475 to 491.

The peptide region containing residues 390-404 in Activated Protein C (APC) is essential for anticoagulant activity and is available for interaction with antibodies or with other proteins, such as the macromolecular substrates Factors Va or VIIIa. APC reg