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SDS-PAGE

PHD finger-like domain-containing protein 5A Recombinant Protein | PHF5A recombinant protein

Recombinant Human PHD finger-like domain-containing protein 5A

Gene Names
PHF5A; INI; Rds3; SF3B7; SAP14b; SF3b14b; bK223H9.2
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
PHD finger-like domain-containing protein 5A; Recombinant Human PHD finger-like domain-containing protein 5A; Splicing factor 3B-associated 14 kDa protein; SF3b14b; PHF5A recombinant protein
Ordering
For Research Use Only!
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
1-110aa; Full Length
Sequence
MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR
Sequence Length
110
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

SDS-PAGE
Related Product Information for PHF5A recombinant protein
Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha. Also involved in pre-mRNA splicing.
Product Categories/Family for PHF5A recombinant protein
References
A genome annotation-driven approach to cloning the human ORFeome.Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.Genome Biol. 5:R84.1-R84.11(2004) The DNA sequence of human chromosome 22.Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.Nature 402:489-495(1999) Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein.Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.EMBO J. 21:4978-4988(2002) Molecular architecture of the multiprotein splicing factor SF3b.Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H.Science 300:980-984(2003) The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome.Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.RNA 10:929-941(2004) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
39.4 kDa
NCBI Official Full Name
PHD finger-like domain-containing protein 5A
NCBI Official Synonym Full Names
PHD finger protein 5A
NCBI Official Symbol
PHF5A
NCBI Official Synonym Symbols
INI; Rds3; SF3B7; SAP14b; SF3b14b; bK223H9.2
NCBI Protein Information
PHD finger-like domain-containing protein 5A
UniProt Protein Name
PHD finger-like domain-containing protein 5A
UniProt Gene Name
PHF5A
UniProt Synonym Gene Names
PHD finger-like domain protein 5A; SF3b14b
UniProt Entry Name
PHF5A_HUMAN

NCBI Description

This gene encodes a subunit of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the intron's branch site in a sequence-independent manner and may anchor the U2 snRNP to the pre-mRNA. The protein encoded by this gene contains a PHD-finger-like domain that is flanked by highly basic N- and C-termini. This protein belongs to the PHD-finger superfamily and may act as a chromatin-associated protein. This gene has several pseudogenes on different chromosomes. [provided by RefSeq, Jul 2008]

Uniprot Description

PHF5A: Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER- alpha. Also involved in pre-mRNA splicing. Belongs to the PHF5 family.

Protein type: RNA-binding; RNA splicing

Chromosomal Location of Human Ortholog: 22q13.2

Cellular Component: nuclear matrix; nuclear speck; nucleoplasm; snRNP U2; U12-dependent spliceosome

Molecular Function: DNA binding; transcription factor activity

Biological Process: gene expression; nuclear mRNA splicing, via spliceosome; positive regulation of transcription, DNA-dependent; RNA splicing; transcription, DNA-dependent

Research Articles on PHF5A

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Product Notes

The PHF5A phf5a (Catalog #AAA1265621) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 1-110aa; Full Length. The amino acid sequence is listed below: MAKHHPDLIF CRKQAGVAIG RLCEKCDGKC VICDSYVRPC TLVRICDECN YGSYQGRCVI CGGPGVSDAY YCKECTIQEK DRDGCPKIVN LGSSKTDLFY ERKKYGFKKR. It is sometimes possible for the material contained within the vial of "PHD finger-like domain-containing protein 5A, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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