Analytical Data
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Gene name
PRKCB
- Application
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Alternative Names
PRKCB; protein kinase C, beta; PKCB, PRKCB1, PRKCB2, protein kinase C, beta 1; protein kinase C beta type; PKC-B; protein kinase C, beta 1 polypeptide; PKCB; PRKCB1; PRKCB2; PKC-beta; MGC41878
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Species
Human
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Source
Baculovirus
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Tag
GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05771-1
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Expression Region
A2-V671
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Protein Length
Full Length of Isoform-1 Mature Protein
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
PRKCB, or Protein Kinase C Beta, is a serine/threonine kinase that plays a crucial role in various cellular processes, including cell proliferation, differentiation, and apoptosis. Its involvement in multiple signaling pathways makes it a significant target for cancer research and other diseases associated with abnormal cell signaling. The reorganization of PRKCB has been studied for its potential implications in therapeutic interventions, particularly in understanding its structure-function relationships. Recent advancements in recombinant protein technology have enabled the production of PRKCB as a well-characterized, functional protein, facilitating detailed investigations into its mechanism of action and interactions with other cellular components. Research has shown that aberrant PRKCB activity is linked to several malignancies, prompting studies aimed at elucidating its role in tumorigenesis. Understanding the structural dynamics and regulatory mechanisms of PRKCB is essential for developing targeted pharmacological strategies and improving the efficacy of existing treatments. Additionally, the exploration of PRKCB's role in various physiological and pathological contexts continues to provide insights into its therapeutic potential, highlighting the need for ongoing research into this important kinase. Overall, the investigation of PRKCB not only enhances our comprehension of cell signaling but also opens avenues for innovative approaches in disease treatment, particularly in cancer and inflammatory disorders.
