protein

Recombinant Human Heterogeneous nuclear ribonucleoprotein K

MBS717395

0.05 mg (E-Coli)

165 USD

Recombinant Protein

Recombinant Human Heterogeneous nuclear ribonucleoprotein K

Heterogeneous nuclear ribonucleoprotein K

Transformation up-regulated nuclear protein; TUNP

heterogeneous nuclear ribonucleoprotein K isoform a; Heterogeneous nuclear ribonucleoprotein K; heterogeneous nuclear ribonucleoprotein K; heterogeneous nuclear ribonucleoprotein K; Transformation up-regulated nuclear protein; TUNP

HNRNPK

HNRPK

HNRNPK; HNRNPK; AUKS; CSBP; TUNP; HNRPK; HNRPK; hnRNP K; TUNP

HNRPK_HUMAN

E Coli

3-459

464

TEQPEETFPNTETNGEFGKRPAEDMEEEQAFKRSRNTDE
MVELRILLQSKNAGAVIGKGGKNIKALRTDYNASVSVPD
SSGPERILSISADIETIGEILKKIIPTLEEGLQLPSPTA
TSQLPLESDAVECLNYQHYKGSDFDCELRLLIHQSLAGG
IIGVKGAKIKELRENTQTTIKLFQECCPHSTDRVVLIGG
KPDRVVECIKIILDLISESPIKGRAQPYDPNFYDETYDY
GGFTMMFDDRRGRPVGFPMRG

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Immunology

One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction. As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. 3 Publications

Characterization and primary structure of the poly(C) -binding heterogeneous nuclear ribonucleoprotein complex K protein.Matunis M.J., Michael W.M., Dreyfuss G.Mol. Cell. Biol. 12:164-171(1992) Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing.Dejgaard K., Leffers H., Rasmussen H.H., Madsen P., Kruse T.A., Gesser B., Nielsen H., Celis J.E.J. Mol. Biol. 236:33-48(1994) Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004)

14165439

NP_002131.2

NM_002140.4

P61978

78.1kD

B Cell Receptor Signaling Pathway (198909); Gene Expression Pathway (1269649); Herpes Simplex Infection Pathway (377873); Herpes Simplex Infection Pathway (377865); Metabolism Of Proteins Pathway (1268677); MicroRNAs In Cancer Pathway (852705); MicroRNAs In Cancer Pathway (852928); Post-translational Protein Modification Pathway (1268701); Processing Of Capped Intron-Containing Pre-mRNA Pathway (1269688); SUMO E3 Ligases SUMOylate Target Proteins Pathway (1268743)

This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene is located in the nucleoplasm and has three repeats of KH domains that binds to RNAs. It is distinct among other hnRNP proteins in its binding preference; it binds tenaciously to poly(C). This protein is also thought to have a role during cell cycle progession. Several alternatively spliced transcript variants have been described for this gene, however, not all of them are fully characterized. [provided by RefSeq, Jul 2008]

hnRNP K: a heterogeneous nuclear ribonucleoprotein (hnRNP). One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Two alternatively spliced isoforms have been described. Protein type: RNA splicing; RNA-binding; Spliceosome. Chromosomal Location of Human Ortholog: 9q21.32-q21.33. Cellular Component: cell cortex; cytoplasm; cytosol; dendritic spine; focal adhesion; membrane; mitochondrion; nerve terminal; nuclear chromatin; nucleoplasm; nucleus; podosome; postsynaptic density. Molecular Function: actinin binding; ATPase binding; heat shock protein binding; lamin binding; mRNA 3'-UTR binding; pre-mRNA 3'-splice site binding; protein binding; protein domain specific binding; ribonucleoprotein binding; RNA binding; single-stranded DNA binding; transcription factor binding. Biological Process: acute-phase response; aging; camera-type eye development; cellular protein metabolic process; cellular response to insulin stimulus; cerebellum development; cerebral cortex development; gene expression; hippocampus development; kidney development; liver development; lung development; negative regulation of apoptosis; negative regulation of nuclear mRNA splicing, via spliceosome; negative regulation of protein binding; negative regulation of transcription from RNA polymerase II promoter; nuclear mRNA splicing, via spliceosome; ovarian follicle development; peripheral nervous system development; positive regulation of low-density lipoprotein receptor biosynthetic process; positive regulation of receptor-mediated endocytosis; positive regulation of RNA splicing; positive regulation of synaptic transmission; positive regulation of transcription from RNA polymerase II promoter; post-translational protein modification; protein sumoylation; response to activity; RNA processing; RNA splicing; signal transduction; thymus development; transcription from RNA polymerase II promoter; viral reproduction. Disease: Au-kline Syndrome

0.05 mg (E-Coli)

165 USD

0.2 mg (E-Coli)

275

0.5 mg (E-Coli)

515

1 mg (E-Coli)

755