Erythropoietin receptor/EpoR Protein, Mouse (sf9, Fc)

Erythropoietin receptor (EpoR) mediates erythropoietin-induced erythroblast proliferation and differentiation. After EPO stimulation, EpoR dimerizes, initiates the JAK2/STAT5 signaling cascade, and can activate STAT1, STAT3, and LYN tyrosine kinases in certain cell types. Erythropoietin receptor/EpoR Protein, Mouse (sf9, Fc) is the recombinant mouse-derived Erythropoietin receptor/EpoR protein, expressed by Sf9 insect cells , with C-hFc labeled tag. The total length of Erythropoietin receptor/EpoR Protein, Mouse (sf9, Fc) is 249 a.a., with molecular weight of ~58.6 kDa.

Erythropoietin receptor (EpoR) serves as the key receptor for erythropoietin, orchestrating erythroblast proliferation and differentiation upon EPO stimulation. Through EpoR dimerization, it initiates the JAK2/STAT5 signaling cascade, leading to various cellular responses. In addition to activating STAT1 and STAT3 in specific cell types, EpoR may also engage the LYN tyrosine kinase. Upon EPO binding, EpoR forms homodimers and undergoes tyrosine phosphorylation, facilitating interactions with diverse SH2 domain-containing proteins such as LYN, APS, PTPN6, PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3, CRKL, and ATXN2L. These interactions, intricate and multifaceted, modulate downstream signaling events, including mitogenic pathways and cell-surface expression. Notably, EpoR's interaction with NOSIP and the ubiquitin ligase NOSIP is implicated in EPO-induced cell proliferation, highlighting the regulatory complexity of EpoR-mediated signaling. Additionally, EpoR forms heterooligomers with FSFFV gp55 and associates with INPP5D/SHIP1, further expanding its functional repertoire in cellular processes.

Mouse

Sf9 insect cells

C-hFc

P14753 (M1-P249)

13857  [NCBI]

MDKLRVPLWPRVGPLCLLLAGAAWAPSPSLPDPKFESKAALLASRGSEELLCFTQRLEDLVCFWEEAASSGMDFNYSFSYQLEGESRKSCSLHQAPTVRGSVRFWCSLPTADTSSFVPLELQVTEASGSPRYHRIIHINEVVLLDAPAGLLARRAEEGSHVVLRWLPPPGAPMTTHIRYEVDVSAGNRAGGTQRVEVLEGRTECVLSNLRGGTRYTFAVRARMAEPSFSGFWSAWSEPASLLTASDLDP

Approximately 58.6 kDa

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.