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SDS-PAGE

Rho GTPase-activating protein 19 Recombinant Protein | ARHGAP19 recombinant protein

Recombinant Human Rho GTPase-activating protein 19

Gene Names
SMARCB1; RDT; INI1; SNF5; Snr1; BAF47; MRD15; RTPS1; Sfh1p; hSNFS; SNF5L1; SWNTS1; PPP1R144
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Rho GTPase-activating protein 19; Recombinant Human Rho GTPase-activating protein 19; BRG1-associated factor 47; BAF47; Integrase interactor 1 protein; SNF5 homolog; hSNF5; ARHGAP19 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
1-494aa; Full Length
Sequence
MMMMALSKTFGQKPVKFQLEDDGEFYMIGSEVGNYLRMFRGSLYKRYPSLWRRLATVEERKKIVASSHGKKTKPNTKDHGYTTLATSVTLLKASEVEEILDGNDEKYKAVSISTEPPTYLREQKAKRNSQWVPTLPNSSHHLDAVPCSTTINRNRMGRDKKRTFPLCFDDHDPAVIHENASQPEVLVPIRLDMEIDGQKLRDAFTWNMNEKLMTPEMFSEILCDDLDLNPLTFVPAIASAIRQQIESYPTDSILEDQSDQRVIIKLNIHVGNISLVDQFEWDMSEKENSPEKFALKLCSELGLGGEFVTTIAYSIRGQLSWHQKTYAFSENPLPTVEIAIRNTGDADQWCPLLETLTDAEMEKKIRDQDRNTRRMRRLANTAPAW
Sequence Length
376
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 ARHGAP19 recombinant protein
Core component of the BAF (hSWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a st/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural st/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural st cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1.
Product Categories/Family for ARHGAP19 recombinant protein
References
Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5.Kalpana G.V., Marmon S., Wang W., Crabtree G.R., Goff S.P.Science 266:2002-2006(1994) Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer.Versteege I., Sevenet N., Lange J., Rousseau-Merck M.-F., Ambros P., Handgretinger R., Aurias A., Delattre O.Nature 394:203-206(1998) The mouse ortholog of the human SMARCB1 gene encodes two splice forms.Bruder C.E., Dumanski J.P., Kedra D.Biochem. Biophys. Res. Commun. 257:886-890(1999) Human Ini1 27bp deletion form.Tozaki H., Yasuda J., Iwakura Y.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) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) NIEHS SNPs programMural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Purification and biochemical heterogeneity of the mammalian SWI-SNF complex.Wang W., Cote J., Xue Y., Zhou S., Khavari P.A., Biggar S.R., Muchardt C., Kalpana G.V., Goff S.P., Yaniv M., Workman J.L., Crabtree G.R.EMBO J. 15:5370-5382(1996) Epstein-Barr virus nuclear protein 2 (EBNA2)binds to a component of the human SNF-SWI complex, hSNF5/Ini1.Wu D.Y., Kalpana G.V., Goff S.P., Schubach W.H.J. Virol. 70:6020-6028(1996) Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region.Morozov A., Yung E., Kalpana G.V.Proc. Natl. Acad. Sci. U.S.A. 95:1120-1125(1998) Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins.Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M., Fornace A.J. Jr., Tkachuk D.C.Mol. Cell. Biol. 19:7050-7060(1999) c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function.Cheng S.-W., Davies K.P., Yung E., Beltran R.J., Yu J., Kalpana G.V.Nat. Genet. 22:102-105(1999) Interaction of E1 and hSNF5 proteins stimulates replication of human papillomavirus DNA.Lee D., Sohn H., Kalpana G.V., Choe J.Nature 399:487-491(1999) Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits.Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.Mol. Cell 3:247-253(1999) Germ-line and acquired mutations of INI1 in atypical teratoid and rhabdoid tumors.Biegel J.A., Zhou J.-Y., Rorke L.B., Stenstrom C., Wainwright L.M., Fogelgren B.Cancer Res. 59:74-79(1999) The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity.Wu D.Y., Tkachuck D.C., Roberson R.S., Schubach W.H.J. Biol. Chem. 277:27706-27715(2002) A key role of the hSNF5/INI1 tumour suppressor in the control of the G1-S transition of the cell cycle.Versteege I., Medjkane S., Rouillard D., Delattre O.Oncogene 21:6403-6412(2002) P16INK4a is required for hSNF5 chromatin remodeler-induced cellular senescence in malignant rhabdoid tumor cells.Oruetxebarria I., Venturini F., Kekarainen T., Houweling A., Zuijderduijn L.M.P., Mohd-Sarip A., Vries R.G.J., Hoeben R.C., Verrijzer C.P.J. Biol. Chem. 279:3807-3816(2004) Chromatin-remodeling factor INI1/hSNF5/BAF47 is involved in activation of the colony stimulating factor 1 promoter.Pan X., Song Z., Zhai L., Li X., Zeng X.Mol. Cells 20:183-188(2005) SMARCB1/INI1 tumor suppressor gene is frequently inactivated in epithelioid sarcomas.Modena P., Lualdi E., Facchinetti F., Galli L., Teixeira M.R., Pilotti S., Sozzi G.Cancer Res. 65:4012-4019(2005) ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.Science 316:1160-1166(2007) 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) Human SWI/SNF generates abundant, structurally altered dinucleosomes on polynucleosomal templates.Ulyanova N.P., Schnitzler G.R.Mol. Cell. Biol. 25:11156-11170(2005) Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex.Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.Genes Dev. 22:2370-2384(2008) Germline mutation of INI1/SMARCB1 in familial schwannomatosis.Hulsebos T.J.M., Plomp A.S., Wolterman R.A., Robanus-Maandag E.C., Baas F., Wesseling P.Am. J. Hum. Genet. 80:805-810(2007) Evidence of a four-hit mechanism involving SMARCB1 and NF2 in schwannomatosis-associated schwannomas.Sestini R., Bacci C., Provenzano A., Genuardi M., Papi L.Hum. Mutat. 29:227-231(2008) Mutations affecting components of the SWI/SNF complex cause Coffin-Siris syndrome.Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y., Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T., Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S., Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.Nat. Genet. 44:376-378(2012)

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
60.1 kDa
NCBI Official Full Name
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 isoform b
NCBI Official Synonym Full Names
SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1
NCBI Official Symbol
SMARCB1
NCBI Official Synonym Symbols
RDT; INI1; SNF5; Snr1; BAF47; MRD15; RTPS1; Sfh1p; hSNFS; SNF5L1; SWNTS1; PPP1R144
NCBI Protein Information
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
UniProt Protein Name
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
UniProt Gene Name
SMARCB1
UniProt Synonym Gene Names
BAF47; INI1; SNF5L1; BAF47; hSNF5
UniProt Entry Name
SNF5_HUMAN

NCBI Description

The protein encoded by this gene is part of a complex that relieves repressive chromatin structures, allowing the transcriptional machinery to access its targets more effectively. The encoded nuclear protein may also bind to and enhance the DNA joining activity of HIV-1 integrase. This gene has been found to be a tumor suppressor, and mutations in it have been associated with malignant rhabdoid tumors. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Dec 2015]

Uniprot Description

SMARCB1: a core component of the BAF (hSWI/SNF) complex. This family of complexes remodels chromatin structures, enabling transcription factors to gain access to DNA. They play important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling is due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4. Involved in activation of CSF1 promoter. Belongs to the neural progenitors- specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain BAF53A and PHF10, are exchanged for homologous alternative BAF53B and BAF45B or BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand- bound VDR-mediated transrepression of the CYP27B1 gene. Component of the BAF (hSWI/SNF) complex, which includes at least actin (ACTB), ARID1A, ARID1B, SMARCA2, SMARCA4, BAF53A, BAF53B, SMARCE1 SMARCC1, SMARCC2, SMARCB1, and one or more of SMARCD1, SMARCD2, or SMARCD3. In muscle cells, the BAF complex also contains DPF3. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Binds to double-stranded DNA. Interacts with EphB4 and MAEL. Interacts with GADD34. Binds tightly to the human immunodeficiency virus-type 1 (HIV-1) integrase in vitro and stimulates its DNA-joining activity. Interacts with human papillomavirus 18 E1 protein to stimulates its viral replication. Belongs to the SNF5 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Tumor suppressor; Transcription, coactivator/corepressor; Cell cycle regulation

Chromosomal Location of Human Ortholog: 22q11.23|22q11

Cellular Component: nuclear chromatin; nucleolus; nucleoplasm; nucleus; protein complex; SWI/SNF complex; XY body

Molecular Function: DNA binding; nucleosomal DNA binding; p53 binding; protein binding; Tat protein binding; transcription coactivator activity

Biological Process: ATP-dependent chromatin remodeling; blastocyst hatching; cell differentiation; chromatin remodeling; DNA integration; DNA repair; establishment and/or maintenance of chromatin architecture; negative regulation of cell proliferation; nervous system development; nucleosome disassembly; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; regulation of transcription from RNA polymerase II promoter; transcription, DNA-dependent

Disease: Mental Retardation, Autosomal Dominant 15; Rhabdoid Tumor Predisposition Syndrome 1; Schwannomatosis 1

Research Articles on ARHGAP19

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Product Notes

The ARHGAP19 smarcb1 (Catalog #AAA1403710) 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 1-494aa; Full Length. The amino acid sequence is listed below: MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER KKIVASSHGK KTKPNTKDHG YTTLATSVTL LKASEVEEIL DGNDEKYKAV SISTEPPTYL REQKAKRNSQ WVPTLPNSSH HLDAVPCSTT INRNRMGRDK KRTFPLCFDD HDPAVIHENA SQPEVLVPIR LDMEIDGQKL RDAFTWNMNE KLMTPEMFSE ILCDDLDLNP LTFVPAIASA IRQQIESYPT DSILEDQSDQ RVIIKLNIHV GNISLVDQFE WDMSEKENSP EKFALKLCSE LGLGGEFVTT IAYSIRGQLS WHQKTYAFSE NPLPTVEIAI RNTGDADQWC PLLETLTDAE MEKKIRDQDR NTRRMRRLAN TAPAW. It is sometimes possible for the material contained within the vial of "Rho GTPase-activating protein 19, 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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