Analytical Data
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Gene name
OBP2B
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简介
The OBP2B protein may be involved in the binding and transport of small hydrophobic volatile molecules, suggesting a role in molecular recognition and transport, especially for lipophilic compounds. Its specificity implies involvement in sensory or signaling pathways in which recognition and transport of volatile compounds are crucial. OBP2B Protein, Human (HEK293, His) is the recombinant human-derived OBP2B protein, expressed by HEK293 , with C-His labeled tag.
- Application
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Alternative Names
Odorant-binding protein 2b; OBPIIb
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Species
Human
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Source
HEK293
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Tag
C-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9NPH6-1
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Expression Region
L16-H170
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Protein Length
Full Length of Isoform-1 Mature Protein
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Molecular Weight
20 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
OBCAM (Oligodendrocyte-Bound Cell Adhesion Molecule) and OPCML (Oligodendrocyte Precursor Cell Market-Like) proteins are significant in the context of neurobiology and cell adhesion research. Both proteins are members of the immunoglobulin superfamily and have been implicated in crucial processes such as oligodendrocyte development, myelination, and neuronal-glial interactions. OBCAM, predominantly expressed in oligodendrocytes, plays a role in myelin sheath formation and maintenance, impacting the overall functionality of the central nervous system. Conversely, OPCML is associated with oligodendrocyte precursor cell regulation and may exert tumor suppressive functions in various cancers, suggesting its broader relevance beyond neurobiology. Research into these proteins has gained momentum due to their potential implications in neurodegenerative diseases, such as multiple sclerosis and amyotrophic lateral sclerosis, where myelin degeneration is a critical factor. Understanding the mechanisms underlying OBCAM and OPCML functions could lead to novel therapeutic strategies aimed at promoting remyelination and restoring neuronal health. Recent advances in recombinant protein technology have enabled the study of these molecules in greater detail, facilitating insights into their structure-function relationships and interactions with other cellular components. As the scientific community continues to explore the biological roles of OBCAM and OPCML, their study represents a promising avenue for advancing our knowledge of neural cell biology and developing targeted therapies for demyelinating conditions.
