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Erythropoietin - CAS 11096-26-7

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Category
Main Product
Product Name
Erythropoietin
Catalog Number
11096-26-7
Synonyms
ERYTHROPOIETIN RAT; EPO; erythropoietin from human urine*approx 100 units; Erythropoietin,from human urine; ERYTHROPOIETIN HUMAN, RECOMB. FROM CHO- CELLS, PGE W. 10 U; ERYTHROPOIETIN FROM HUMAN URINE*APPROX 5 00 UNITS PE; ERYTHROPOIETIN FROM HUMAN URINE*APPROX
CAS Number
11096-26-7
Description
Produced by the kidneys,this glycoprotein is involved in red blood cell production. It has a predicted molecular mass of ~21 kDa but migrates at ~37 kDa on SDS-PAGE.
Molecular Weight
0
Quantity
Milligrams-Grams
Quality Standard
In-house Standard
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MSDS
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Sequence
Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg
Size Price Stock Quantity
1 mg $499 In stock

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Structure
CAS 11096-26-7 Erythropoietin
Specification
Physical Description
Erythropoietin, Human Recombinant (50 units)
Application
For research used only
Storage
Store at -20ºC Freezer
Reference Reading
1.Evaluation of the osteogenesis and angiogenesis effects of erythropoietin and the efficacy of deproteinized bovine bone/recombinant human erythropoietin scaffold on bone defect repair
Donghai Li • Liqing Deng • Xiaowei Xie • Zhouyuan Yang • Pengde Kang. J Mater Sci: Mater Med (2016) 27:101
Vascular formation is conducted primarily by vascular growth factors, among which, vascular endothelial growth factor (VEGF) is the most effective one. Studies have found that erythropoietin (EPO) can increase the expression of VEGF and promote the angiogenesis. Meanwhile, it may also play a role in bone regeneration. EPO has been used in clinic with its anti-apoptotic and tissueprotective effects in treatment of chronic anemia, myocardial infraction, diabetes mellitus, spinal cord injury, acute lung injury, et al. for ages. Studies showed that EPO can increase the VEGF expression in the injury sites, help to form the vessel and heal the wound. According to Kim’s vitro trial, EPO can promote the mesenchymal stem cells to differentiate into osteoblast. In the recent studies, recombinant human erythropoietin (rhEPO) was administered in mice to repair the femoral segmental defect, and the results showed that EPO exerts prominent effects of enhancing bone formation, cell proliferation and increasing the VEGF-mediated angiogenesis.
2.Erythropoietin and erythropoietin-receptor producing cells demonstrated by in situ hybridization in mouse visceral yolk sacs
Yoshiko Yasuda, Masaki Okano, Masaya Nagao. 58 Anatomical Science International (2002) 77, 58–63
The visceral yolk sac (VYS) is the first site of erythropoiesis in amniota, including in humans. The primitive erythropoiesis in the VYS has been demonstrated to be incomplete dependency on erythropoietin (EPO), while the definitive erythropoiesis in the fetal liver has been demonstrated to have complete dependency on EPO in knockout mouse embryos targeted for EPO and/or erythropoietin-receptor (EPOR) gene (Wu et al., 1995; Lin et al., 1996). The EPO gene has been demonstrated in VYSs on day 7.5 of gestation in mice by whole-mount methods of in situ hybridization (Rich et al., 1994), and immunoreactive EPO and EPOR proteins have been shown to be present in the extraembryonic endoderm and VYS on days 6–8 of gestation (Yasuda et al., 1993). Using reverse transciption polymerase chain reaction (RT–PCR) methods, we discovered the temporary expression of mRNAs for EPO and EPOR in mice VYSs on days 9–11 of gestation (Yasuda et al., 1996). However, the exact site of EPO- and EPOR-synthesizing cells has not been identified, and we have not identified which cells in the VYS are involved in EPO secretion or whether EPO–EPOR signal transduction operates by an autocrine or paracrine pathway in the VYS. In this paper, we show that by in situ hybridization, EPO mRNA can be seen in adjacent endodermal cells in a group, and that EPOR mRNA is present in the majority of endodermal and mesodermal cells. Considering the locations of immunoreactive EPO and EPOR protein in the VYS, approximately half of the endodermal epithelial cells appear to produce EPO and most cell components to synthesize EPOR. The EPO–EPOR signal appears to operate in both autocrine and paracrine pathways in the VYS.
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