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Recombinant human PKC beta 1 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS, WB.

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Images

Western blot - Recombinant human PKC beta 1 protein (AB60840), expandable thumbnail
  • Functional Studies - Recombinant human PKC beta 1 protein (AB60840), expandable thumbnail
  • SDS-PAGE - Recombinant human PKC beta 1 protein (AB60840), expandable thumbnail
  • Western blot - Recombinant human PKC beta 1 protein (AB60840), expandable thumbnail
  • Functional Studies - Recombinant human PKC beta 1 protein (AB60840), expandable thumbnail

Publications

Key facts

Purity
>90% Densitometry
Expression system
Baculovirus infected Sf9 cells
Tags
GST tag N-Terminus
Applications
SDS-PAGE, FuncS, WB
Biologically active
Yes

Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Application
FuncS
Reactivity
Reacts
Dilution info
-
Notes

-

Application
WB
Reactivity
Reacts
Dilution info
-
Notes

ab60840 can be used as a WB positive control in conjunction with ab4132.

Target data

Function

Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity (PubMed:11598012). Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A (PubMed:20228790). In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1 (PubMed:25982116). Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (PubMed:19176525). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231).

Alternative names

PKCB, PRKCB1, PRKCB, Protein kinase C beta type, PKC-B, PKC-beta

Recommended products

Recombinant human PKC beta 1 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS, WB.

Key facts

Purity
>90% Densitometry
Expression system
Baculovirus infected Sf9 cells
Applications
SDS-PAGE, FuncS, WB
Biological activity
Specific Activity: 283 nmol/min/mg
Accession
P05771-1
Animal free
No
Species
Human
Concentration
Loading...
Storage buffer

pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.0038% EGTA, 0.00292% EDTA, 0.00174% PMSF

Sequence info

Amino acid sequence

Accession
P05771
Protein length
Full Length
Nature
Recombinant
Tags
GST tag N-Terminus

Specifications

Form
Liquid
Additional notes

Purity: >90% as determined by densitometry. Affinity purified.

General info

Function

Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity (PubMed:11598012). Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A (PubMed:20228790). In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1 (PubMed:25982116). Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (PubMed:19176525). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231).

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Post-translational modifications

Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Autophosphorylation on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade (By similarity).

Subcellular localisation
Nucleus

Storage

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

This product is an active protein and may elicit a biological response in vivo, handle with caution.

Notes

PKC epsilon peptide ab204875 (PKC epsilon peptide) can be utilized as a substrate for assessing kinase activity

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

PKC beta 1 (Protein Kinase C beta 1) is an enzyme that belongs to the protein kinase C (PKC) family. It plays an important role in signal transduction processes. This protein has a molecular mass of approximately 80 kDa and is known to express in various tissues including the brain heart and spleen. PKC beta 1 undergoes phosphorylation upon activation which alters its structure and function. It localizes to the cytoplasm and also to the cellular membranes under certain conditions.

Biological function summary

PKC beta 1 is involved in regulating various cellular functions such as cell survival differentiation and proliferation. It operates as part of a larger kinase complex and influences downstream targets via its catalytic activity. The activity of PKC beta 1 impacts cytoskeleton reorganization and vesicular trafficking. It interacts with other PKC isoforms and different substrates contributing significantly to cellular homeostasis.

Pathways

PKC beta 1 plays a major role in the MAPK/ERK and PI3K/AKT pathways. These pathways are essential for transmitting signals from growth factors and hormones to cellular responses. PKC protein's interaction within these pathways involves modulation of other proteins like Raf-1 and Akt which are critical for executing biological outcomes. PKC beta 1 through its influence in these pathways partakes in controlling cell fate decisions.

Associated diseases and disorders

PKC beta 1 has connections to diabetic complications and certain cancers. Its altered expression or dysregulation links with the progression of diabetic retinopathy by impacting vascular endothelial growth factor (VEGF) production. Additionally atypical PKC beta 1 signaling contributes to tumorigenesis in cancers like chronic lymphocytic leukemia. PKC protein’s aberrant activity in these conditions associates with altered survival pathways and resistance to apoptosis.

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