Recombinant Human Endocrine Gland Vascular Endothelial Growth Factor

SKU:BHP11002554
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ProSpec-Tany TechnoGene Ltd
ProSpec-Tany TechnoGene Ltd
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Overview
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RUO recombinant Endocrine Gland Vascular Endothelial Growth Factor (Human) protein for mechanistic studies and assay development. Supplied as a traceable protein input (E. coli; >95% (SDS-PAGE) purity; lyophilized; MW 9.7 kDa) for reproducible assay inputs.
Target PRK1
Species Human
Options selector
Catalog no. Size
cyt-338-5UG 5 ug
cyt-338-20UG 20 ug
cyt-338-1MG 1 mg
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) — 5 ug, 20 ug, 1 mg
  • Lead time: options listed as “in stock at manufacturer” typically ship in 5–7 business days; other statuses may take longer.
  • Storage: Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No cyt-338
Alternative Names PK1, PRK1, Prokineticin 1, EG-VEGF.
Biological Activity The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
Cellular Localization Cell membrane
Concentration 1 mg/ml
Expression System
  • E. coli
Form Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).
Product Type
  • Proteins & Peptides
  • Cytokines and Growth Factors
Protein Length 86
Protein Size 9.7 kDa
Purity Greater than 95.0% as determined by SDS-PAGE.
Solubility It is recommended to reconstitute the lyophilized Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Source Escherichia Coli.
Species Human
Storage Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Target PRK1

Recombinant Human Endocrine Gland Vascular Endothelial Growth Factor is supplied as a recombinant protein for in vitro research use.

Background

Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.

Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications Abstract: Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent. Introduction: Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders. Production and Characterization: Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF. Role in Endocrine Disorders: EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases. Therapeutic Implications: Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies. Conclusion: Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.

Product format

Provided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.

What is the purity of Recombinant Human Endocrine Gland Vascular Endothelial Growth Factor (Human)?
Greater than 95.0% as determined by SDS-PAGE. BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
What buffer / formulation is this protein supplied in?
Supplied as: The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA). Reconstitute lyophilized material in sterile ultrapure water or the recommended buffer per the datasheet prior to use.
How should Recombinant Human Endocrine Gland Vascular Endothelial Growth Factor (Human) be stored?
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles. Prepare single-use aliquots after reconstitution to avoid repeated freeze–thaw cycles.
What expression system was used to produce this protein?
This recombinant protein was expressed in E. coli. The system was selected to achieve high yield, correct folding, and appropriate post-translational modifications.
Is this protein biologically active?
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml. Refer to the product datasheet for recommended assay conditions and controls.
Is this protein approved for clinical or in vitro diagnostic use?
No. Supplied for Research Use Only (RUO) — not intended for therapeutic applications or in vitro diagnostic procedures.
Can I request a custom size, tag variant, or formulation?
Yes. BioHippo can accommodate custom requests including alternative sizes, His/GST/Fc tag variants, bulk quantities, and custom formulations. See the Customization & Add-ons tab or email support@biohippo.com.

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

Bibliography: Ferrara, N., & Davis-Smyth, T. (1997). The biology of vascular endothelial growth factor. Endocrine Reviews, 18(1), 4-25. Helmbrecht, G. D., & Soares, M. J. (1998). Effects of endocrine vascular endothelial growth factor (VEGF) on placental development. Theriogenology, 49(1), 155. Kholová, I., & Kautzner, J. (2013). Molecular mechanisms of cardiac lymphangiogenesis: From development to heart failure. Heart Failure Reviews, 18(6), 703-716. LeCouter, J., Zlot, C., Tejada, M., et al. (2001). Bv8 and endocrine gland-derived vascular endothelial growth factor stimulate hematopoiesis and hematopoietic cell mobilization. Proceedings of the National Academy of Sciences, 98(11), 748-753. Persico, M. G., & Di Palma, T. (2007). Structure, expression and receptor-binding properties of placenta growth factor (PlGF). Current Pharmaceutical Design, 13(28), 2945-2951.
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