Human FRP-5, soluble

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Cat-Nr.S01-077S
Size10 µg
Price95 €
SourceCHO cells
Formulationlyophilized
Purity Confirmation≥ 98% by SDS-PAGE gel and HPLC analyses
Length [aa]288
Molecular Weight32.7 kDa
Endotoxin Levels< 0.1 ng/µg of protein (<1EU/µg)
Biological ActivityDetermined by its ability to decrease alkaline phosphatase activity in CCL-226 cells when treated with 25 ng/ml of Murine Wnt-3a.
SynonymsSecreted frizzled‐related protein 5, Frizzled‐related protein 1b, FRP‐1b, Secreted apoptosis‐related protein 3, SARP‐3
DescriptionSecreted Frizzled Related Proteins (sFRPs) are a family of glycosylated Wnt antagonists that inhibit Wnt signaling, either by directly binding to Wnt proteins to prevent their binding to Frizzled (Fz) family receptor proteins or by forming non‐functional interactions with Frizzled receptors. sFRPs share homology with the cysteine‐rich, extracellular domain of Frizzled proteins. sFRP‐5 is secreted in a variety of embryonic and adult tissues. During embryonic development, sFRP‐5 regulates formation of the retina, brain, trunk, foregut, anterior visceral endoderm, and epithelial structures through Wnt and BMP inhibition. In adults, sFRP‐5 is expressed by adipocytes, particularly in white adipose tissue, and acts as an anti‐inflammatory adipokine. Shown to improve metabolic function and reduce adipose tissue inflammation, sFRP‐5 also acts in a cardio‐protective manner after ischemia and reperfusion injury in the heart, suppressing the non‐canonical Wnt5a/JNK signaling pathway in macrophages and myocytes. sFRP‐5 levels are negatively correlated with obesity‐related disorders including insulin resistance, type 2 diabetes, dyslipidemia, atherosclerosis, and coronary artery disease. Downregulation by promoter hypermethylation is observed in numerous cancers including gastric, cervical, hepatocellular carcinoma, pancreatic, oral squamous cell, breast, colon, bladder, and renal. sFRP‐5 inhibits melanogenesis when expressed in vitiligo melanocytes. CHO cell‐derived Recombinant Human sFRP5 is a 288‐amino‐acid length glycoprotein with a calculated molecular weight of 32.7 kDa; however, due to glycosylation, protein migration occurs at an apparent molecular weight of approximately 33‐35 kDa by SDS‐PAGE analysis under both reducing and non‐reducing conditions.
Protein SequenceEEYDYYGWQA EPLHGRSYSK PPQCLDIPAD LPLCHTVGYK RMRLPNLLEH ESLAEVKQQA SSWLPLLAKR CHSDTQVFLC SLFAPVCLDR PIYPCRSLCE AVRAGCAPLM EAYGFPWPEM LHCHKFPLDN DLCIAVQFGH LPATAPPVTK ICAQCEMEHS ADGLMEQMCS SDFVVKMRIK EIKIENGDRK LIGAQKKKKL LKPGPLKRKD TKRLVLHMKN GAGCPCPQLD SLAGSFLVMG RKVDGQLLLM AVYRWDKKNK EMKFAVKFMF SYPCSLYYPF FYGAAEPH
Uniprot IDQ5T4F7
Protein RefSeqNP_003006.2
mRNA RefSeqNM_003015.3

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