Recombinant Human FAM20C Protein (Tagged)

Name: Recombinant Human FAM20C Protein (Tagged)
Brand: Beta LifeScience
SKU: BLA-3472P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	Q8IXL6
Synonym	C76981 Dentin matrix protein 4 DKFZp547C074 DMP-4 DMP4 DMP4_HUMAN Extracellular serine/threonine protein kinase Fam20C Fam20c Family with sequence similarity 20 member C GEF CK Golgi enriched fraction casein kinase Protein FAM20C RNS
Description	Recombinant Human FAM20C Protein (Tagged) was expressed in Mammalian. It is a Full length protein
Source	Mammalian
AA Sequence	DFSSDPSSNLSSHSLEKLPPAAEPAERALRGRDPGALRPHDPAHRPLLRD PGPRRSESPPGPGGDASLLARLFEHPLYRVAVPPLTEEDVLFNVNSDTRL SPKAAENPDWPHAGAEGAEFLSPGEAAVDSYPNWLKFHIGINRYELYSRH NPAIEALLHDLSSQRITSVAMKSGGTQLKLIMTFQNYGQALFKPMKQTRE QETPPDFFYFSDYERHNAEIAAFHLDRILDFRRVPPVAGRMVNMTKEIRD VTRDKKLWRTFFISPANNICFYGECSYYCSTEHALCGKPDQIEGSLAAFL PDLSLAKRKTWRNPWRRSYHKRKKAEWEVDPDYCEEVKQTPPYDSSHRIL DVMDMTIFDFLMGNMDRHHYETFEKFGNETFIIHLDNGRGFGKYSHDELS ILVPLQQCCRIRKSTYLRLQLLAKEEYKLSLLMAESLRGDQVAPVLYQPH LEALDRRLRVVLKAVRDCVERNGLHSVVDDDLDTEHRAASAR
Molecular Weight	66 kDa
Purity	>90% by SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilised
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs and plays a key role in biomineralization of bones and teeth. Constitutes the main protein kinase for extracellular proteins, generating the majority of the extracellular phosphoproteome. Mainly phosphorylates proteins within the Ser-x-Glu/pSer motif, but also displays a broader substrate specificity. Phosphorylates casein as well as a number of proteins involved in biomineralization such as AMELX, AMTN, ENAM and SPP1. In addition to its role in biomineralization, also plays a role in lipid homeostasis, wound healing and cell migration and adhesion.
Subcellular Location	Secreted. Golgi apparatus.
Protein Families	FAM20 family
Database References	HGNC: 22140 OMIM: 259775 KEGG: hsa:56975 STRING: 9606.ENSP00000322323 UniGene: Hs.134742
Associated Diseases	Raine syndrome (RNS)
Tissue Specificity	Widely expressed.

Gene Functions References

that FAM20C may affect the biomineralization by the means more than local phosphorylation of extracellular matrix proteins and systemic phosphorus homeostasis PMID: 28926103
Histidine-rich Ca-binding protein (HRC) was phosphorylated by family with sequence similarity 20C (Fam20C) both in vitro and in vivo. PMID: 28784772
These results suggest that TET1 potentially promotes the cytodifferentiation potential of human dental pulp cells through its DNA demethylation machinery and upregulation of FAM20C protein expression. PMID: 29277934
findings clarify FAM20C's role in hard tissue formation and mineralization, and show that Raine syndrome is congenital sclerosing osteomalacia with cerebral calcification. PMID: 27862258
Alterations of Fam20C activity, promoted by myriocin and sphingolipids, are not accompanied by any significant change in Fam20C protein. These data provide the proof of concept that Fam20C activity is under the control of sphingolipid signaling PMID: 28236661
Our report reinforces that Raine syndrome is compatible with life, and that mild hypophosphatemia and amelogenesis imperfecta are key features of the attenuated form. PMID: 27667191
The Fam20C-and VLK-family of kinases mediate the phosphorylation of proteins in the secretory pathway and extracellular space.Mutation in several secretory pathway kinases cause human disease PMID: 25862977
by treating Fam20C expressing HEK293T cells with myriocin, a potent inhibitor of the sphingosine biosynthetic pathway, the activity of Fam20C released into the conditioned medium is substantially decreased corroborating the concept that sphingosine PMID: 25936777
Using CRISPR/Cas9 genome editing, mass spectrometry, and biochemistry, study identifies more than 100 secreted phosphoproteins as genuine Fam20C substrates; further, study shows that Fam20C exhibits broader substrate specificity than previously appreciated. PMID: 26091039
phenotype in two families with non-lethal Raine syndrome with FAM20C mutations PMID: 25928877
Findings suggest that certain homozygous FAM20C mutations can cause FGF23-related hypophosphatemic osteomalacia and indicate the multiple roles of FAM20C in bone. PMID: 24982027
Results suggest that FAM20C suppresses FGF23 production by enhancing DMP1 expression, and inactivating mutations in FAM20C cause FGF23-related hypophosphatemia by decreasing transcription of DMP1. PMID: 25026495
We report on a child who is homozygous for a 487-kb deletion in 7p22.3 that contains FAM20C PMID: 24039075
Fam20C phosphorylates FGF23, which promotes FGF23 proteolysis by furin by blocking O-glycosylation by polypeptide N-acetylgalactosaminyltransferase 3. PMID: 24706917
mutations in FAM20C provide a putative new mechanism in human subjects leading to dysregulated FGF23 levels, hypophosphatemia, hyperphosphaturia, dental anomalies, intracerebral calcifications and osteosclerosis of the long bones PMID: 23325605
Our results identify FAM20C as a kinase for secreted phosphoproteins and establish a biochemical basis for Raine syndrome. PMID: 22900076
Fam20C appears to be the Golgi casein kinase that phosphorylates secretory pathway proteins within S-x-E motifs; Fam20C phosphorylates caseins and several secreted proteins implicated in biomineralization; mutations in Fam20C cause an osteosclerotic bone dysplasia known as Raine syndrome PMID: 22582013
Osteosclerotic bone dysplasia in siblings with a Fam20C mutation PMID: 20825432
This study defines the causative role of FAM20C in this lethal osteosclerotic disorder and its crucial role in normal bone development. PMID: 17924334
Mutation of FAM20C does not always lead to the infantile lethality previously seen as a prerequisite for Raine syndrome diagnosis. PMID: 19250384

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.