Analytical Data
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Gene name
APLP-2
- Application
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Alternative Names
APPH; APPL2; CDEBP; Amyloid protein homolog; CDEI box-binding protein
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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 95% as determined by SDS-PAGE.
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Uniprot
Q06481
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Expression Region
Met1~Gly210
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Molecular Weight
34kDa
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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
ULBP1 (UL16 binding protein 1) is a critical member of the ULBP family, which consists of ligands that engage with the NKG2D receptor on natural killer (NK) cells and certain T cells. The expression of ULBP1 is often induced in response to stress, infection, or malignancy, making it a significant player in the immune response, particularly in tumor immunology. Research has shown that ULBP1 interacts with various cellular pathways that modulate immune evasion and tumor progression, suggesting its potential role as a therapeutic target or biomarker in cancer immunotherapy. The recombinant expression of ULBP1 offers a valuable tool for studying its functions and mechanisms of action. Creating ULBP1 as a recombinant protein allows researchers to examine its structure, binding affinities, and effects on immune cell activation. Additionally, understanding the post-translational modifications of ULBP1 through recombinant methods can shed light on its regulatory mechanisms in the immune system. The development of ULBP1-recombinant proteins has also paved the way for novel therapeutic strategies, including engineered NK cell therapies and immune checkpoint inhibitors designed to enhance anti-tumor responses. Overall, the study of recombinant ULBP1 contributes significantly to the understanding of host-pathogen interactions, immune regulation, and the design of innovative cancer treatments.
