Analytical Data
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Gene name
HHIPL1
- Application
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96JK4
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Expression Region
20-782aa
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Molecular Weight
90.9 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
HHIPL1, or HHIP-like protein 1, has garnered considerable attention in the field of molecular biology and biomedicine due to its potential role in various physiological and pathological processes. Recently, studies have suggested that HHIPL1 may be involved in cellular signaling pathways, particularly those related to cell proliferation and differentiation. The understanding of HHIPL1’s function has been bolstered by its resemblance to the hedgehog signaling pathway, which is crucial for embryonic development and tissue homeostasis. Dysregulation of this pathway has been implicated in several cancers, making HHIPL1 a candidate for further investigation as a potential biomarker or therapeutic target. Furthermore, research has indicated that HHIPL1 may play a role in modulating inflammation and tissue repair mechanisms, which highlights its relevance in chronic diseases. The recombinant protein expression of HHIPL1 allows for the exploration of its biological functions through in vitro and in vivo studies, facilitating the elucidation of its mechanisms of action. This approach not only aids in the discovery of new therapeutic strategies but also contributes to the understanding of its involvement in disease processes. As such, research on HHIPL1 and its recombinant protein form could provide insights into novel treatment options for conditions associated with aberrant hedgehog signaling and related pathways, underscoring the significance of this protein in contemporary biomedical research.
