Filaggrin (FLG) Recombinant Protein | FLG recombinant protein

Recombinant Human Filaggrin (FLG), partial

Cat. Num. AAA967523

• Gene Names: FLG; ATOD2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Filaggrin (FLG); Recombinant Human Filaggrin (FLG); partial; FLG recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 3838-4061aa; Partial
• Sequence: DSSRHSQSGQGESAGSRRSRRQGSSVSQDSDSEAYPEDSERRSESASRNHHGSSREQSRDGSRHPGSSHRDTASHVQSSPVQSDSSTAKEHGHFSSLSQDSAYHSGIQSRGSPHSSSSYHYQSEGTERQKGQSGLVWRHGSYGSADYDYGESGFRHSQHGSVSYNSNPVVFKERSDICKASAFGKDHPRYYATYINKDPGLCGHSSDISKQLGF SQSQRYYYYE

• Production Note: Special Offer: The Yeast host-expressed protein is manufactured from a stock plasmid containing the protein gene. Yeasthost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The Yeast host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select Yeast host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for FLG recombinant protein

Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis.

Product Categories/Family for FLG recombinant protein

Signal Transduction

References

The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Characterization of the human epidermal profilaggrin gene. Genomic organization and identification of an S-100-like calcium binding domain at the amino terminus.Presland R.B., Haydock P.V., Fleckman P., Nirunsuksiri W., Dale B.A.J. Biol. Chem. 267:23772-23781(1992) Characterization of a cDNA clone encoding human filaggrin and localization of the gene to chromosome region 1q21.McKinley-Grant L.J., Idler W.W., Bernstein I.A., Parry D.A.D., Cannizzaro L., Croce C.M., Huebner K., Lessin S.R., Steinert P.M.Proc. Natl. Acad. Sci. U.S.A. 86:4848-4852(1989) Identification of the amino terminus of human filaggrin using differential LC/MS techniques implications for profilaggrin processing.Thulin C.D., Walsh K.A.Biochemistry 34:8687-8692(1995) Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis.Senshu T., Kan S., Ogawa H., Manabe M., Asaga H.Biochem. Biophys. Res. Commun. 225:712-719(1996) Loss-of-function variations within the filaggrin gene predispose for atopic dermatitis with allergic sensitizations.Weidinger S., Illig T., Baurecht H., Irvine A.D., Rodriguez E., Diaz-Lacava A., Klopp N., Wagenpfeil S., Zhao Y., Liao H., Lee S.P., Palmer C.N.A., Jenneck C., Maintz L., Hagemann T., Behrendt H., Ring J., Nothen M.M., McLean W.H.I., Novak N.J. Allergy Clin. Immunol. 118:214-219(2006) Filaggrin loss-of-function mutations predispose to phenotypes involved in the atopic march.Marenholz I., Nickel R., Rueschendorf F., Schulz F., Esparza-Gordillo J., Kerscher T., Grueber C., Lau S., Worm M., Keil T., Kurek M., Zaluga E., Wahn U., Lee Y.-A.J. Allergy Clin. Immunol. 118:866-871(2006) Loss-of-function mutations in the gene encoding filaggrin cause ichthyosis vulgaris.Smith F.J.D., Irvine A.D., Terron-Kwiatkowski A., Sandilands A., Campbell L.E., Zhao Y., Liao H., Evans A.T., Goudie D.R., Lewis-Jones S., Arseculeratne G., Munro C.S., Sergeant A., O'Regan G., Bale S.J., Compton J.G., DiGiovanna J.J., Presland R.B., Fleckman P., McLean W.H.I.Nat. Genet. 38:337-342(2006) Common loss-of-function variants of the epidermal barrier protein filaggrin are a major predisposing factor for atopic dermatitis.Palmer C.N.A., Irvine A.D., Terron-Kwiatkowski A., Zhao Y., Liao H., Lee S.P., Goudie D.R., Sandilands A., Campbell L.E., Smith F.J.D., O'Regan G.M., Watson R.M., Cecil J.E., Bale S.J., Compton J.G., DiGiovanna J.J., Fleckman P., Lewis-Jones S., Arseculeratne G., Sergeant A., Munro C.S., El Houate B., McElreavey K., Halkjaer L.B., Bisgaard H., Mukhopadhyay S., McLean W.H.I.Nat. Genet. 38:441-446(2006) Unique mutations in the filaggrin gene in Japanese patients with ichthyosis vulgaris and atopic dermatitis.Nomura T., Sandilands A., Akiyama M., Liao H., Evans A.T., Sakai K., Ota M., Sugiura H., Yamamoto K., Sato H., Palmer C.N.A., Smith F.J.D., McLean W.H.I., Shimizu H.J. Allergy Clin. Immunol. 119:434-440(2007) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)

NCBI and Uniprot Product Information

• NCBI GI #: 60097902
• NCBI GeneID: 2312
• NCBI Accession #: NP_002007.1
• NCBI GenBank Nucleotide #: NM_002016.1
• UniProt Accession #: P20930; Q01720; Q5T583; Q9UC71
• Molecular Weight: 26.8 kDa
• NCBI Official Full Name: filaggrin
• NCBI Official Synonym Full Names: filaggrin
• NCBI Official Symbol: FLG
• NCBI Official Synonym Symbols: ATOD2
• NCBI Protein Information: filaggrin
• UniProt Protein Name: Filaggrin
• Protein Family: Filaggrin
• UniProt Gene Name: FLG
• UniProt Entry Name: FILA_HUMAN

NCBI Description

The protein encoded by this gene is an intermediate filament-associated protein that aggregates keratin intermediate filaments in mammalian epidermis. It is initially synthesized as a polyprotein precursor, profilaggrin (consisting of multiple filaggrin units of 324 aa each), which is localized in keratohyalin granules, and is subsequently proteolytically processed into individual functional filaggrin molecules. Mutations in this gene are associated with ichthyosis vulgaris.[provided by RefSeq, Dec 2009]

Uniprot Description

FLG: Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis. Defects in FLG are the cause of ichthyosis vulgaris (VI); also known as ichthyosis simplex. Ichthyosis vulgaris is the most common form of ichthyosis inherited as an autosomal dominant trait. It is characterized by palmar hyperlinearity, keratosis pilaris and a fine scale that is most prominent over the lower abdomen, arms, and legs. Ichthyosis vulgaris is characterized histologically by absent or reduced keratohyalin granules in the epidermis and mild hyperkeratosis. The disease can be associated with frequent asthma, eczema or hay fever. Defects in FLG are a cause of susceptibility to dermatitis atopic type 2 (ATOD2). Atopic dermatitis is a complex, inflammatory disease with multiple alleles at several loci thought to be involved in the pathogenesis. It commonly begins in infancy or early childhood and is characterized by a chronic relapsing form of skin inflammation, a disturbance of epidermal barrier function that culminates in dry skin, and IgE- mediated sensitization to food and environmental allergens. It is manifested by lichenification, excoriation, and crusting, mainly on the flexural surfaces of the elbow and knee. Belongs to the S100-fused protein family.

Protein type: Cytoskeletal

Chromosomal Location of Human Ortholog: 1q21.3

Cellular Component: intermediate filament; intracellular membrane-bound organelle; nucleus

Molecular Function: calcium ion binding; protein binding; structural molecule activity

Biological Process: keratinocyte differentiation; multicellular organismal development

Disease: Dermatitis, Atopic, 2; Ichthyosis Vulgaris