Comparison

Recombinant Human Heterogeneous nuclear ribonucleoprotein A1(HNRNPA1),partial

Item no. CSB-EP010600HU-10
Manufacturer Cusabio
Amount 10ug
Category
Type Proteins Recombinant
Format Liquid or Lyophilized powder
Specific against other
Host E.coli
Purity Greater than 90% as determined by SDS-PAGE.
ECLASS 10.1 32160409
ECLASS 11.0 32160409
UNSPSC 12352202
Alias Helix-destabilizing protein;Single-strand RNA-binding proteinhnRNP core protein A1
Available
Research areas
Immunology
Target / Protein
HNRNPA1
Biologically active
Not Test
Expression system
E.coli
Species of origin
Homo sapiens (Human)
Uniprot ID
P09651
AA Sequence
SKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQ WGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAA MNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKK IFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRG SGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCE VRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFG GNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNG FGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGY GGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFG NYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKP RNQ
Tag Info
N-terminal 6xHis-tagged
Expression Region
2-354aa
Protein length
Partial
MW
40.9 kDa
Alternative Name(s)
Helix-destabilizing protein; Single-strand RNA-binding proteinhnRNP core protein A1
Relevance
Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.
References
The finished DNA sequence of human chromosome 12.Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006)
Purity
Greater than 90% as determined by SDS-PAGE.
Storage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week.
Function
Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection
Involvement in disease
Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 3 (IBMPFD3); Amyotrophic lateral sclerosis 20 (ALS20)
Subcellular Location
Nucleus, Cytoplasm, Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs, Shuttles continuously between the nucleus and the cytoplasm along with mRNA, Component of ribonucleosomes (PubMed:17289661), SUBCELLULAR LOCATION: Cytoplasm
Tag Information
N-terminal 6xHis-tagged

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 10ug
Available: In stock
available

Compare

Add to wishlist

Get an offer

Request delivery time

Ask a technical question

Submit a bulk request

Questions about this Product?
 
Close