Analytical Data
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Gene name
PHYHIPL
- Application
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Alternative Names
PHYHIPL; KIAA1796; UNQ6309/PRO20934Phytanoyl-CoA hydroxylase-interacting protein-like
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96FC7
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Expression Region
1-376 aa
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AA Sequence
MEVPRLDHAL NSPTSPCEEV IKNLSLEAIQ LCDRDGNKSQ DSGIAEMEEL PVPHNIKISN ITCDSFKISW EMDSKSKDRI THYFIDLNKK ENKNSNKFKH KDVPTKLVAK AVPLPMTVRG HWFLSPRTEY TVAVQTASKQ VDGDYVVSEW SEIIEFCTAD YSKVHLTQLL EKAEVIAGRM LKFSVFYRNQ HKEYFDYVRE HHGNAMQPSV KDNSGSHGSP ISGKLEGIFF SCSTEFNTGK PPQDSPYGRY RFEIAAEKLF NPNTNLYFGD FYCMYTAYHY VILVIAPVGS PGDEFCKQRL PQLNSKDNKF LTCTEEDGVL VYHHAQDVIL EVIYTDPVDL SVGTVAEITG HQLMSLSTAN AKKDPSCKTC NISVGR
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Molecular Weight
42.4 kDa
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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
PHYHIPL, a member of the phytochrome-interacting protein family, has garnered significant attention in recent years due to its role in plant signaling pathways and development. Initially identified as a protein that interacts with phytochromes—red and far-red light receptors—PHYHIPL is believed to modulate plant growth responses to light, making it a crucial player in photomorphogenesis. Studies have suggested that PHYHIPL may influence processes such as seed germination, stem elongation, and leaf expansion by regulating the expression of light-responsive genes. Moreover, understanding the mechanisms through which PHYHIPL operates can provide insights into how plants adapt to their environments, particularly in the context of changing light conditions. Given the increasing interest in agricultural biotechnology and crop improvement, research into PHYHIPL is particularly relevant as it may help in developing strategies for enhancing plant resilience and productivity under varying environmental stresses. Recent advances in molecular biology techniques have facilitated the investigation of PHYHIPL's structure, function, and genetic regulation, further emphasizing its importance in the field of plant science. Overall, the study of PHYHIPL not only contributes to our understanding of fundamental plant biology but also holds potential for practical applications in sustainable agriculture.
