Analytical Data
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Gene name
SEMA3G
- Application
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Alternative Names
Semaphorin sem2
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Species
Human
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Source
HEK293
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NS98
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Expression Region
23-782aa
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Molecular Weight
89.5 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
SEMA3G, a member of the semaphorin protein family, plays a crucial role in a variety of biological processes, particularly in the nervous system. Semaphorins, originally identified for their function in axon guidance during neuronal development, have since been implicated in numerous other physiological and pathological phenomena, including immune response and tumorigenesis. SEMA3G is primarily known for its role as a chemorepulsive signal, influencing the migration and organization of neurons and other cells. Recent studies have highlighted its involvement in modulating angiogenesis and regulating immune cell functions, suggesting broader implications in both developmental biology and disease states. Moreover, alterations in SEMA3G expression levels have been associated with various cancers, underscoring its potential as a biomarker and therapeutic target. Understanding the functional mechanisms of SEMA3G, including its interactions with receptors such as neuropilins and plexins, can provide insights into its roles in cell signaling pathways. The characterization of SEMA3G as a recombinant protein for research purposes allows scientists to explore these pathways in controlled experimental settings, enabling the examination of its effects on different cell types and interactions within the tumor microenvironment. Overall, the study of SEMA3G and its recombinant forms represents a promising area of investigation that could lead to advancements in targeted therapies for cancer and other diseases influenced by semaphorin signaling.
