Analytical Data
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Gene name
HN1L
- Application
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Alternative Names
JPT2;C16orf34;HN1L;Jupiter microtubule associated homolog 2
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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
Q9H910
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Expression Region
1-190aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFQVPDS EGGRAGSRAM KPPGGESSNL FGSPEEATPS SRPNRMASNI FGPTEEPQNI PKRTNPPGGK GSGIFDESTP VQTRQHLNPP GGKTSDIFGS PVTATSRLAH PNKPKDHVFL CEGEEPKSDL KAARSIPAGA EPGEKGSARK AGPAKEQEPM PTVDSHEPRL GPRPRSHNKV LNPPGGKSSI SFY
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Molecular Weight
23 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
HN1L, or HN1-like protein, is a member of the heterokaryon-inducing (HN) protein family that has garnered attention in the field of molecular biology and biomedicine due to its potential role in various cellular processes. Research has indicated that HN1L is involved in the regulation of cell growth, differentiation, and apoptosis, making it a candidate for studying diseases such as cancer and neurodegenerative disorders. The protein is believed to participate in the modulation of key signaling pathways, influencing cellular responses to stress and nutrient availability. Furthermore, adaptations in the expression levels or functional dynamics of HN1L have been observed in pathological conditions, underscoring its relevance as a biomarker and therapeutic target. With advancements in recombinant protein technology, the production and characterization of HN1L in vitro have become feasible, enabling researchers to delve deeper into its biochemical properties and interactions. Understanding the structure-function relationships of HN1L through recombinant studies can provide insight into its roles in health and disease, paving the way for potential applications in disease modeling and drug development. The exploration of HN1L's mechanisms may ultimately contribute to the development of innovative therapeutic strategies aimed at targeting the underlying causes of diseases associated with its dysregulation.
