Recombinant Human PHIP protein is a Human Fragment protein, in the 1146 to 1287 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
M H H H H H H S L I Y K P L D G E W G T N P R D E E C E R I V A G I N Q L M T L D I A S A F V A P V D L Q A Y P M Y C T V V A Y P T D L S T I K Q R L E N R F Y R R V S S L M W E V R Y I E H N T R T F N E P G S P I V K S A K F V T D L L L H F I K D Q T C Y N I I P L Y N S M K K K V L S D S E D E E
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization.
Alternative names
DCAF14, WDR11, PHIP, PH-interacting protein, DDB1- and CUL4-associated factor 14, IRS-1 PH domain-binding protein, WD repeat-containing protein 11
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Recombinant Human PHIP protein is a Human Fragment protein, in the 1146 to 1287 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- Q8WWQ0-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.02% Potassium chloride
Sequence info
Amino acid sequence
- M H H H H H H S L I Y K P L D G E W G T N P R D E E C E R I V A G I N Q L M T L D I A S A F V A P V D L Q A Y P M Y C T V V A Y P T D L S T I K Q R L E N R F Y R R V S S L M W E V R Y I E H N T R T F N E P G S P I V K S A K F V T D L L L H F I K D Q T C Y N I I P L Y N S M K K K V L S D S E D E E
- Accession
- Q8WWQ0
- Protein length
- Fragment
- Predicted molecular weight
- 17 kDa
- Amino acids
- 1146 to 1287
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
General info
- Function
Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization.
- Subcellular localisation
- Nucleus
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
PHIP also known as pleckstrin homology domain interacting protein is an adapter protein that interacts with insulin receptor substrates. It has a mass of approximately 100 kDa. PHIP is expressed in various tissues including the brain and liver. The protein is involved in intracellular signaling pathways by binding phosphoinositides which are important for cellular communication and growth regulation.
- Biological function summary
PHIP plays a significant role in cell proliferation and survival. It contributes to the regulation of the cell cycle by influencing transcription factors and other core components involved in cell growth. PHIP is not only a standalone protein but also part of complexes that modulate chromatin affecting gene expression patterns.
- Pathways
PHIP is integrated into insulin signaling and PI3K/AKT pathways. In these pathways PHIP interacts with key proteins like AKT1 supporting cellular responses to insulin and growth factors. The involvement of PHIP in these pathways highlights its role in metabolic regulation and its impact on cell growth and metabolism.
- Associated diseases and disorders
PHIP has links to cancer and diabetes. Its dysregulation contributes to abnormal cell proliferation often observed in cancers. PHIP's interaction with insulin signaling components such as IRS1 demonstrates its relevance to diabetes management. These connections show PHIP's potential as a therapeutic target for these conditions.
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1 product image
SDS-PAGE - Recombinant Human PHIP protein (ab196110)
4-20% SDS-PAGE analysis of 2.3 μg ab196110 with Coomassie staining.
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