SFRP4 Human
Secreted Frizzled-Related Protein 4 Human Recombinant
Cat. No.
BT20545
Source
HEK 293.
Synonyms
Secreted frizzled-related protein 4, sFRP-4, Frizzled protein, human endometrium, FrpHE, SFRP4, FRPHE, FRP-4.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
SFRP4 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 19-346) containing a total of 341 amino acids, having a molecular mass of 39kDa (calculated), though it migrates at approximately 55kDa on SDS PAGE, the SFRP4 is fused to a 5 a.a N-terminal linker and an 8 a.a Flag tag at N-Terminus.
The Human SFRP4 is purified by proprietary chromatographic techniques.
The Human SFRP4 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Secreted frizzled-related protein 4 (SFRP4) is a member of the SFRP family, characterized by a cysteine-rich domain similar to the Wnt-binding site on Frizzled proteins. Acting as soluble Wnt signaling regulators, SFRPs, particularly SFRP4, might govern adult uterine morphology and function. SFRP4 potentially elevates apoptosis during ovulation, possibly by interacting with FZ1/FZ4/WNT4 signaling. Additionally, SFRP4 demonstrates phosphaturic effects through targeted inhibition of sodium-dependent phosphate uptake. Expression of SFRP4 is observed in proliferative endometrium, various ovarian, endometrial, and breast tumors. Notably, SFRP4 is present in mesenchymal cells and cardiomyocytes, with its expression in ventricular myocardium correlating with apoptosis-related gene activity. Elevated SFRP4 levels are observed in failing myocardium.
Description
Recombinant Human SFRP4, produced in HEK cells, is a single, glycosylated polypeptide chain encompassing amino acids 19-346. This totals 341 amino acids, resulting in a calculated molecular mass of 39kDa. However, it exhibits a migration pattern corresponding to approximately 55kDa on SDS-PAGE. This discrepancy is attributed to glycosylation. The SFRP4 construct includes a 5 amino acid N-terminal linker and an 8 amino acid Flag tag at the N-terminus. Purification of Human SFRP4 is achieved through proprietary chromatographic techniques.
Physical Appearance
White lyophilized powder after filtration.
Formulation
The product is sterile filtered (0.4µm) and lyophilized. The initial solution contains 0.5mg/ml of SFRP4 in a buffer composed of 0.05M phosphate buffer and 0.075M NaCl, at a pH of 7.4.
Solubility
To prepare a working solution, add deionized water to achieve a concentration of 0.5mg/ml. Allow the lyophilized pellet to dissolve completely. Note: SFRP4 is not sterile. Before using in cell culture, filter the product through a sterile filter with an appropriate pore size.
Stability
Store the lyophilized SFRP4 protein at -20°C. After reconstitution, aliquot the product to minimize repeated freeze-thaw cycles. While the reconstituted protein can be stored at 4°C for a limited period, it is recommended to use it within two weeks as no changes are observed within this timeframe.
Purity
The purity of SFRP4 is determined to be greater than 90.0% using SDS-PAGE analysis.
Synonyms
Secreted frizzled-related protein 4, sFRP-4, Frizzled protein, human endometrium, FrpHE, SFRP4, FRPHE, FRP-4.
Source
HEK 293.
Amino Acid Sequence
PGDYKDDDDK PAGVRGAPCE AVRIPMCRHM PWNITRMPNH LHHSTQENAI LAIEQYEELV DVNCSAVLRF FLCAMYAPIC TLEFLHDPIK PCKSVCQRAR DDCEPLMKMY NHSWPESLAC DELPVYDRGV CISPEAIVTD LPEDVKWIDI TPDMMVQERP LDVDCKRLSP DRCKCKKVKP TLATYLSKNY SYVIHAKIKA VQRSGCNEVT TVVDVKEIFK SSSPIPRTQV PLITNSSCQC PHILPHQDVL IMCYEWRSRM MLLENCLVEK WRDQLSKRSI QWEERLQEQR RTVQDKKKTA GRTSRSNPPK PKGKPPAPKP ASPKKNIKTR SAQKRTNPKR V.
Product Science Overview
Gene and Protein Structure
The SFRP4 gene is located on chromosome 7 at position 7p14.1 in humans . The gene encodes a protein that is secreted into the extracellular space and functions as a modulator of Wnt signaling . The protein structure includes a cysteine-rich domain that is crucial for its interaction with Wnt proteins .
Biological Functions
SFRP4 plays a significant role in various biological processes, including:
- Regulation of Wnt Signaling: SFRP4 acts as an antagonist of the Wnt signaling pathway, which is essential for cell proliferation, differentiation, and apoptosis .
- Apoptosis and Cancer: SFRP4 has been shown to be pro-apoptotic and anti-angiogenic, making it a potential target for cancer therapy . It can sensitize cancer stem cells to chemotherapeutic drugs, thereby improving the efficacy of cancer treatments .
- Bone Morphogenesis: SFRP4 is involved in bone morphogenesis and phosphate ion homeostasis . Biallelic, recessive variants in the SFRP4 gene can result in Pyle disease, a genetic disorder characterized by a failure of long bone remodeling and increased bone fragility .
- Type 2 Diabetes: SFRP4 is a hub gene in a Type 2 Diabetes-associated gene coexpression module in human islets. It reduces glucose-induced insulin secretion through decreased β-cell exocytosis .
Clinical Implications
- Cancer Therapy: SFRP4’s role in sensitizing cancer stem cells to chemotherapy highlights its potential as a therapeutic target . By inhibiting the Wnt/β-catenin signaling pathway, SFRP4 can reduce the proliferative capacity of cancer stem cells and improve chemo-responses .
- Bone Disorders: The association between SFRP4 deficiency and Pyle disease underscores the importance of SFRP4 in bone health and its potential as a target for treating bone disorders .
- Diabetes Management: Elevated levels of SFRP4 in serum have been observed several years before the clinical diagnosis of Type 2 Diabetes, suggesting its potential as a biomarker for early detection and management of the disease .
Research and Development
Ongoing research is focused on understanding the molecular mechanisms by which SFRP4 modulates Wnt signaling and its broader implications in various diseases. The development of recombinant SFRP4 proteins and their potential therapeutic applications are areas of active investigation.
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