Protein-arginine deiminase type-1 Recombinant Protein | PADI1 recombinant protein

Recombinant Human Protein-arginine deiminase type-1

Cat. Num. AAA1331963

• Gene Names: PADI1; PDI; PAD1; PDI1; HPAD10
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Protein-arginine deiminase type-1; Recombinant Human Protein-arginine deiminase type-1; Peptidylarginine deiminase I; Protein-arginine deiminase type I; PADI1 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: 1-663aa; Full Length
• Sequence: MAPKRVVQLSLKMPTHAVCVVGVEAHVDIHSDVPKGANSFRVSGSSGVEVFMVYNRTRVKEPIGKARWPLDTDADMVVSVGTASKELKDFKVRVSYFGEQEDQALGRSVLYLTGVDISLEVDTGRTGKVKRSQGDKKTWRWGPEGYGAILLVNCDRDNHRSAEPDLTHSWLMSLADLQDMSPMLLSCNGPDKLFDSHKLVLNVPFSDSKRVRVFCARGGNSLSDYKQVLGPQCLSYEVERQPGEQEIKFYVEGLTFPDADFLGLVSLSVSLVDPGTLPEVTLFTDTVGFRMAPWIMTPNTQPPEELYVCRVMDTHGSNEKFLEDMSYLTLKANCKLTICPQVENRNDRWIQDEMEFGYIEAPHKSFPVVFDSPRNRGLKDFPYKRILGPDFGYVTREIPLPGPSSLDSFGNLDVSPPVTVGGTEYPLGRILIGSSFPKSGGRQMARAVRNFLKAQQVQAPVELYSDWLSVGHVDEFLTFVPTSDQKGFRLLLASPSACLKLFQEKKEEGYGEAAQFDGLKHQAKRSINEMLADRHLQRDNLHAQKCIDWNRNVLKRELGLAESDIVDIPQLFFLKNFYAEAFFPDMVNMVVLGKYLGIPKPYGPIINGRCCLEEKVQSLLEPLGLHCIFIDDYLSYHELQGEIHCGTNVRRKPFPFKWWNMVP
• Sequence Length: 663

• 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 PADI1 recombinant protein

Catalyzes the deimination of arginine residues of proteins.

Product Categories/Family for PADI1 recombinant protein

Epigenetics and Nuclear Signaling

References

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I.Guerrin M., Ishigami A., Mechin M.-C., Nachat R., Valmary S., Sebbag M., Simon M., Senshu T., Serre G.Biochem. J. 370:167-174(2003) Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6.Chavanas S., Mechin M.-C., Takahara H., Kawada A., Nachat R., Serre G., Simon M.Gene 330:19-27(2004) 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)

NCBI and Uniprot Product Information

• NCBI GI #: 122056685
• NCBI GeneID: 29943
• NCBI Accession #: NP_037490.2
• NCBI GenBank Nucleotide #: NM_013358.2
• UniProt Accession #: Q9ULC6; Q70SX6; A1L4K6
• Molecular Weight: 76.7 kDa
• NCBI Official Full Name: protein-arginine deiminase type-1
• NCBI Official Synonym Full Names: peptidyl arginine deiminase, type I
• NCBI Official Symbol: PADI1
• NCBI Official Synonym Symbols: PDI; PAD1; PDI1; HPAD10
• NCBI Protein Information: protein-arginine deiminase type-1
• UniProt Protein Name: Protein-arginine deiminase type-1
• Protein Family: Protein-arginine deiminase
• UniProt Gene Name: PADI1
• UniProt Synonym Gene Names: PAD1; PDI1
• UniProt Entry Name: PADI1_HUMAN

NCBI Description

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type I enzyme is involved in the late stages of epidermal differentiation, where it deiminates filaggrin and keratin K1, which maintains hydration of the stratum corneum, and hence the cutaneous barrier function. This enzyme may also play a role in hair follicle formation. This gene exists in a cluster with four other paralogous genes. [provided by RefSeq, Jul 2008]

Uniprot Description

PADI1: Catalyzes the deimination of arginine residues of proteins. Epidermis, prostate, testis, placenta, spleen and thymus. Belongs to the protein arginine deiminase family.

Protein type: Hydrolase; EC 3.5.3.15

Chromosomal Location of Human Ortholog: 1p36.13

Cellular Component: cytoplasm

Molecular Function: calcium ion binding; protein-arginine deiminase activity

Biological Process: peptidyl-citrulline biosynthetic process from peptidyl-arginine