Recombinant AREG Human Protein [E.coli.] (MAG-2295)

AREG Human Protein

MAG-2295

His

Escherichia Coli.

At Room Temperature

Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa. The AREG is purified by proprietary chromatographic techniques.

Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

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Sterile Filtered White lyophilized (freeze-dried) powder.

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

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 .

Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

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.

SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

Mabioway's Co., Ltd products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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.

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.