Analytical Data
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Gene name
HNT
- Application
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Alternative Names
hNT; IgLON family member 2; IGLON2; Neurotrimin; NT; NTM; NTRI_HUMAN
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Species
Human
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Source
E. coli
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Tag
His tag C-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9P121
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Expression Region
1-312aa
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AA Sequence
MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID NRVTRVAWLN RSTILYAGND KWCLDPRVVL LSNTQTQYSI EIQNVDVYDE GPYTCSVQTD NHPKTSRVHL IVQVSPKIVE ISSDISINEG NNISLTCIAT GRPEPTVTWR HISPKAVGFV SEDEYLEIQG ITREQSGDYE CSASNDVAAP VVRRVKVTVN YPPYISEAKG TGVPVGQKGT LQCEASAVPS AEFQWYKDDK RLIEGKKGVK VENRPFLSKL IFFNVSEHDY GNYTCVASNK LGHTNASIML FG
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Molecular Weight
32 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
HNT (Hemahtin-Nucleotide Transporter) recombinant protein research has gained significant attention due to its crucial role in cellular metabolism and potential therapeutic applications. HNT is implicated in the transport of essential nucleotides, which are vital for various cellular functions including energy metabolism, signaling pathways, and nucleic acid synthesis. Understanding the structure and function of HNT can provide insights into its mechanisms of action and regulatory processes in human health and disease. Additionally, abnormalities in nucleotide transport have been linked to several pathological conditions, including metabolic disorders and cancer. The production of HNT as a recombinant protein allows for detailed studies of its biochemical properties, interactions, and role in cellular processes, paving the way for the development of targeted drugs and treatment strategies. Furthermore, the use of recombinant technologies to produce HNT can facilitate the investigation of its potential as a biomarker for disease progression and response to therapy, opening new avenues for precision medicine. As researchers continue to explore the implications of HNT in both physiology and pathology, the findings could lead to innovative approaches in drug development and enhance our understanding of nucleotide metabolism in various biological contexts. Overall, the study of HNT recombinant protein represents a promising frontier in biomedical research with the potential for significant clinical impact.
