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Recombinant Human Amphiregulin protein (rFc Tag)

种属

Human

纯度

>85 %, SDS-PAGE

标签

rFc Tag

生物活性

未测试

Cat no : Eg4569

Print datasheet

Synonyms

AREG, AR, AREGB, Colorectum cell-derived growth factor, CRDGF

验证数据展示

  • Purity of Recombinant Human Amphiregulin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Human Amphiregulin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

产品信息

纯度 >85 %, SDS-PAGE
内毒素 <0.1 EU/μg protein, LAL method
生物活性 Not tested
来源 HEK293-derived Human Amphiregulin protein Ser101-Lys187 (Accession# P15514) with a rabbit IgG Fc tag at the N-terminus.
基因ID 374
蛋白编号 P15514
预测分子量 37.3 kDa
SDS-PAGE 10-16 kDa and 37-48 kDa, reducing (R) conditions
组分 Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
复溶 Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
储存条件
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
运输条件 The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

背景信息

Amphiregulin (AREG) is one of the ligands of the epidermal growth factor receptor (EGFR). AREG plays a central role in mammary gland development and branching morphogenesis in organs and is expressed both in physiological and in cancerous tissues. The AREG protein is synthesized as a 252-amino acid transmembrane precursor, pro-AREG. At the plasma membrane, pro-AREG is subjected to sequential proteolytic cleavages within its ectodomain and is then released as the soluble AREG protein. Depending on the cell type and microenvironment, AREG can be produced in multiple cellular and mature forms using alternative pro-AREG cleavage sites and glycosylation motifs.

参考文献:

1. Brown C.L., et al. (1998). J Biol Chem. Jul 3;273(27):17258-17268.
2. Busser B, et al. (2011). Biochim Biophys Acta. Dec;1816(2):119-131. 
3. McBryan J, et al. (2008). J Mammary Gland Biol Neoplasia. Jun;13(2):159-69.