Analytical Data
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Gene name
VEGFB
- Application
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Alternative Names
VEGFB；VRF；Vascular endothelial growth factor B
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Species
Human
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Source
HEK293
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Tag
GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49765
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Expression Region
1-207aa
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AA Sequence
MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA
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Molecular Weight
41,6 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
Identification
Protein Description
Vascular endothelial growth factor B (VEGFB) is a member of the VEGF family, primarily known for its role in angiogenesis and maintaining vascular homeostasis. Unlike other VEGF isoforms, VEGFB primarily acts on lymphatic endothelium and is crucial for the development and survival of endothelial cells. Recent studies have highlighted its involvement in various physiological processes, including lipid metabolism, neuroprotection, and cardiac function. Research has shown that VEGFB can promote the survival of damaged neurons and enhance cardiac repair following ischemic injury, suggesting its potential therapeutic implications for cardiovascular and neurodegenerative diseases. Given its significant role in these biological processes, the recombinant protein form of VEGFB is being investigated for its potential applications in drug development and regenerative medicine. Scientists are particularly interested in characterizing VEGFB's structure-function relationships to explore its mechanism of action, optimize its therapeutic properties, and assess its efficacy in preclinical models. Furthermore, understanding the interaction between VEGFB and its receptors could unveil new pathways for treatment strategies aimed at diseases characterized by inadequate blood supply or impaired tissue repair. Overall, the study of VEGFB recombinant proteins has garnered attention due to their promise in enhancing tissue regeneration and their ability to modulate vascular responses, making them a focal point in contemporary biomedical research.
