Recombinant Human Amphiregulin

SKU:BHP11002457
Suppliers
ProSpec-Tany TechnoGene Ltd
ProSpec-Tany TechnoGene Ltd
Details Products
Overview
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RUO recombinant Amphiregulin (Human) protein for mechanistic studies and assay development. Supplied as a traceable protein input (E. coli; >95% (SDS-PAGE) purity; lyophilized; MW 11.3 kDa) for reproducible assay inputs.
Target MGC13647
Species Human
Options selector
Catalog no. Size
cyt-041-10UG 10 ug
cyt-041-50UG 50 ug
cyt-041-1MG 1 mg
Available Options

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

  • Options: Size (3) — 10 ug, 50 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 AREG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AREG should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). 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-041
Alternative Names Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.
Biological Activity Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED 50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.
Expression System
  • E. coli
Form Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.
Product Type
  • Proteins & Peptides
  • Cytokines and Growth Factors
  • Other Protein
Protein Length 98
Protein Size 11.3 kDa
Purity Greater than 95.0% as determined by:<br>(a) Analysis by HPLC.<br>(b) Analysis by SDS-PAGE.
Solubility It is recommended to reconstitute the lyophilized AREG in sterile 18M-cm H 2 O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Source Escherichia Coli.
Species Human
Storage Lyophilized AREG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AREG should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles .
Target MGC13647

Recombinant Human Amphiregulin is supplied as a recombinant protein for in vitro research use.

Background

Amphiregulin Human Recombinant: Exploring its Role in Cancer Biology and Therapeutic Applications Abstract: Amphiregulin, a member of the epidermal growth factor (EGF) family, has gained significant attention in cancer research. This research paper provides an overview of Amphiregulin human recombinant, highlighting its molecular characteristics, signaling pathways, and therapeutic potential. Understanding the multifaceted role of Amphiregulin opens avenues for targeted cancer therapies. This article provides a concise analysis of Amphiregulin, emphasizing its impact on cancer biology and its therapeutic applications. Introduction: Cancer continues to be a significant health challenge worldwide, necessitating novel therapeutic approaches. Amphiregulin, an EGF family member, has emerged as a promising target in cancer research. This paper provides an overview of Amphiregulin, shedding light on its structure, function, and therapeutic potential. Amphiregulin Signaling and Mechanisms: Amphiregulin exerts its effects through the binding and activation of the EGF receptor (EGFR). Upon activation, a cascade of intracellular signaling pathways is triggered, including the MAPK and PI3K/AKT pathways. These pathways regulate critical cellular processes such as cell proliferation, survival, migration, and angiogenesis. Amphiregulin in Cancer Biology: Amphiregulin has been implicated in various aspects of cancer biology, including tumor growth, metastasis, and resistance to therapy. Its overexpression is observed in several cancer types, and its role in promoting tumor growth and metastasis has been demonstrated in preclinical studies. Targeting Amphiregulin signaling shows promise in inhibiting cancer progression and overcoming therapy resistance. Therapeutic Potential of Amphiregulin Human Recombinant: Amphiregulin human recombinant holds significant therapeutic potential in cancer treatment. Strategies aimed at blocking Amphiregulin-EGFR interactions or inhibiting downstream signaling pathways are being explored as potential therapeutic interventions. Additionally, Amphiregulin could serve as a predictive biomarker to identify patients who are more likely to respond to targeted therapies. Challenges and Future Directions: While the therapeutic targeting of Amphiregulin shows promise, several challenges need to be addressed. Further research is required to fully understand the complex interplay between Amphiregulin and other molecular pathways in cancer biology. Additionally, the development of specific and potent inhibitors and the identification of patient selection criteria are important considerations for successful clinical translation. Conclusion: Amphiregulin human recombinant represents a promising avenue for targeted cancer therapy. Understanding the molecular mechanisms and functional implications of Amphiregulin in cancer biology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve patient outcomes and contribute to the advancement of personalized medicine.

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 Amphiregulin (Human)?
Greater than 95.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis 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: Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4. Reconstitute lyophilized material in sterile ultrapure water or the recommended buffer per the datasheet prior to use.
How should Recombinant Human Amphiregulin (Human) be stored?
Lyophilized AREG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AREG should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). 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?
Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED 50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg. 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.

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Experience the power of Celltrypse™, c-LEcta's innovative enzyme solution for gentle and efficient cell dissociation. Request your free sample and discover a superior alternative for your cell culture workflows.

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