Pkc Iota [Pt555]/Pkc Lambda [Pt563]
The PKC family of serine⁄threonine kinases, including PRKCI (PKC iota), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR4742A
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCI (PKC iota), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3607
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCG (PKC gamma), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR1467A
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCG (PKC gamma), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3604
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCB1 (PKC beta I), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR1458A
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCB1 (PKC beta I), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3601
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCA (PKC alpha), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR1455C
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCA (PKC alpha), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3600
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCB2 (PKC beta II), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR1461C
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCB2 (PKC beta II), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3602
Size: 1 mg
Size: 1 mg
PRKC1 (PKC mu) is a serine⁄threonine protein kinase that is phospholipid-dependant and activated by diacylglycerol and phorbol ester TPA. PRKC1 behaves similarly to most PKC isoenzymes of the PKC family, however, PRKC1 differs in some structural and enzymatic features from the other PKC isotypes, and has been shown to be involved in the signal transduction of a wide range of biological responses.
Catalog: PR7258C
Size: 100 µg
Size: 100 µg
PRKC1 (PKC mu) is a serine⁄threonine protein kinase that is phospholipid-dependant and activated by diacylglycerol and phorbol ester TPA. PRKC1 behaves similarly to most PKC isoenzymes of the PKC family, however, PRKC1 differs in some structural and enzymatic features from the other PKC isotypes, and has been shown to be involved in the signal transduction of a wide range of biological responses.
Catalog: PV4041
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCZ (PKC zeta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR1476D
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCZ (PKC zeta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3606
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCQ (PKC theta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR4143B
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCQ (PKC theta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3605
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCD (PKC delta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR1464B
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCD (PKC delta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3603
Size: 1 mg
Size: 1 mg
The PKC family of serine⁄threonine kinases, including PRKCH (PKC eta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PR3588A
Size: 100 µg
Size: 100 µg
The PKC family of serine⁄threonine kinases, including PRKCH (PKC eta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent.
Catalog: PV3608
Size: 1 mg
Size: 1 mg
Pkc Iota [Pt555]/Pkc Lambda [Pt563]
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Previous: pkc inhibitors | Next: Pkc Theta [Pt538]
