Analytical Data
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Gene name
PHYHIP
- Application
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Alternative Names
PHYHIP; DYRK1AP3; KIAA0273; Phytanoyl-CoA hydroxylase-interacting protein; Phytanoyl-CoA hydroxylase-associated protein 1; PAHX-AP1; PAHXAP1
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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
Q92561
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Expression Region
1-330 aa
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AA Sequence
MELLSTPHSI EINNITCDSF RISWAMEDSD LERVTHYFID LNKKENKNSN KFKHRDVPTK LVAKAVPLPM TVRGHWFLSP RTEYSVAVQT AVKQSDGEYL VSGWSETVEF CTGDYAKEHL AQLQEKAEQI AGRMLRFSVF YRNHHKEYFQ HARTHCGNML QPYLKDNSGS HGSPTSGMLH GVFFSCNTEF NTGQPPQDSP YGRWRFQIPA QRLFNPSTNL YFADFYCMYT AYHYAILVLA PKGSLGDRFC RDRLPLLDIA CNKFLTCSVE DGELVFRHAQ DLILEIIYTE PVDLSLGTLG EISGHQLMSL STADAKKDPS CKTCNISVGR
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Molecular Weight
37.5 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
Related Products
Protein Description
The study of phytohemagglutinin (PHA) recombinant proteins, specifically PHYHIP, is rooted in the need to understand the molecular mechanisms underlying plant lectins and their potential applications in biotechnology and medicine. PHA is a well-known lectin derived from the kidney bean, Phaseolus vulgaris, and has been extensively studied for its ability to agglutinate cells and its role in plant defense mechanisms. PHYHIP, a specific recombinant variant of PHA, has garnered attention due to its unique properties and interactions with various biological systems. Research on PHYHIP focuses on its structural characteristics, binding affinities, and functional roles in immunology and cell biology. The recombinant production of PHYHIP allows for enhanced yield and functionality compared to its native form, making it a valuable tool for studying cell signaling, immune responses, and even as a potential therapeutic agent in cancer treatment and vaccine development. Furthermore, understanding the interactions of PHYHIP with glycosylated surfaces offers insights into cell-cell communication and pathogen recognition, fostering advancements in both fundamental research and practical applications. This area of research continues to expand as scientists explore the potential of PHYHIP in various fields, from agricultural biotechnology to clinical therapeutics.
