Recombinant Human U1 Small Nuclear Ribonucleoprotein 70 Kda (SNRNP70) Protein (His)

Beta LifeScience SKU/CAT #: BLC-02112P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human U1 Small Nuclear Ribonucleoprotein 70 Kda (SNRNP70) Protein (His)

Beta LifeScience SKU/CAT #: BLC-02112P
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Product Overview

Description Recombinant Human U1 Small Nuclear Ribonucleoprotein 70 Kda (SNRNP70) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P08621
Target Symbol SNRNP70
Synonyms SNRNP70; RNPU1Z; RPU1; SNRP70; U1AP1U1 small nuclear ribonucleoprotein 70 kDa; U1 snRNP 70 kDa; U1-70K; snRNP70
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRH
Expression Range 1-210aa
Protein Length Partial
Mol. Weight 28.7 kDa
Research Area Epigenetics And Nuclear Signaling
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA.; Truncated isoforms that lack the RRM domain cannot bind U1-snRNA.; Truncated isoforms that lack the RRM domain cannot bind U1-snRNA.
Subcellular Location Nucleus speckle. Nucleus, nucleoplasm.
Database References

HGNC: 11150

OMIM: 180740

KEGG: hsa:6625

STRING: 9606.ENSP00000472998

UniGene: PMID: 27105840

  • The epitopes of U1-70K autoantibodies have been mapped at single-amino acid resolution. PMID: 26333287
  • The authors propose that Gemin2 is a versatile hub for ribonucleoprotein exchange that functions broadly in RNA metabolism. PMID: 26828962
  • data lead to a model that FUS functions in coupling transcription to splicing via mediating an interaction between RNAP II and U1 snRNP PMID: 26124092
  • The selection of 5'-splice site nucleotides by U1 snRNP is achieved predominantly through basepairing with U1 snRNA whilst U1-C fine-tunes relative affinities of mismatched 5'-splice sites. PMID: 25555158
  • methylation of snRNP70 by SETMAR regulates constitutive and/or alternative splicing PMID: 25795785
  • U1-70K interacts with the SMN complex and is required for nuclear gem integrity. PMID: 25052091
  • Data indicate that small nuclear ribonucleoprotein U1-70K in Alzheimer disease (AD) may directly sequester normal soluble forms of U1-70K into insoluble aggregates. PMID: 25355317
  • [review] The presence of antibodies against U1snRNP autoantigen is considered the serological hallmark of mixed connective tissue disease (MCTD), which is characterized by overlapping features between at least two systemic autoimmune diseases. PMID: 24461387
  • These studies identify U1 snRNP pathologic changes in brain of early onset genetic forms of Alzheimer's disease PMID: 24773620
  • inhibition of U1 snRNP also leads to regulation of the usage of In3 pA, suggesting that the C/P activity in the cell can be cross-regulated by splicing, leading to coordination between these two processes. PMID: 23874216
  • Our results demonstrate unique U1 snRNP pathology and implicate abnormal RNA splicing in Alzheimer's disease pathogenesis. PMID: 24023061
  • High expression of U1-70K and other U1 small nuclear ribonucleoproteins spliceosome proteins in Alzheimer's disease patients and those with mild cognitive impairment. PMID: 24023061
  • Serum antibodies against the 70k polypeptides of the U1 ribonucleoprotein complex are associated with psychiatric syndromes in systemic lupus erythematosus. PMID: 22454191
  • U1-snRNP activates the NOD-like receptor family, pyrin domain-containing 3 (NLRP3) inflammasome in CD14+ human monocytes dependently of anti-U1-snRNP Abs, leading to interleukin (IL)-1beta production. PMID: 22490866
  • data identify some fungal proteins as possible triggers of anti-U1-70 kDa autoimmunity via molecular mimicry. PMID: 21348812
  • the hypo-phosphorylated RS domain of SRSF1 interacts with its own RRM, thus competing with U1-70K binding, whereas the hyper-phosphorylated RS domain permits the formation of a ternary complex containing ESE, an SR protein, and U1 snRNP PMID: 21536904
  • Recruitment of RNAPII, U1-70K and ASF/SF2 protein to transcription sites is splicing independent. PMID: 20519584
  • crucial association of B19-NS1 in development of autoimmunity by inducing apoptosis and specific cleavage of 70 kDa U1-snRNP PMID: 20500824
  • U1-70k isoforms control subunit dynamics in the human spliceosomal U1 snRNP PMID: 19784376
  • Apoptotic U1-70 kd is antigenically distinct from the intact form of the U1-70-kd molecule. PMID: 12115232
  • A remarkably limited and consistent pattern of T cell targeting of U1-70kDa in connective tissue disease patients is observed in T cell clones generated against U1-70kDa: all clones are specific for epitopes within the RNA binding domain of the protein. PMID: 12218166
  • Apoptotic modification and the presence of an RNA binding domain may both contribute to autoantigenicity of the lupus U1-70-kDa ribonucleoprotein. PMID: 14688384
  • Specific binding of heterogenous nuclear ribonucleoprotein E1 (hnRNP E1) and U1 small nuclear ribonucleoprotein (snRNP) in the pre-spliceosomal complex was associated with silencing of pseudoexon splicing. PMID: 17622584
  • Examine changes in phosphorylation/dephosphorylation balance and the subcellular localization of the U1-70K protein during apoptosis. PMID: 18202700
  • In a transgenic model of mixed connective tissue disease, T cell recognition of the U1 70-kDa autoantigen by HLA-DR4-transgenic mice is focused on a limited number of T cell epitopes residing primarily within the RNA-binding domain of the RNP autoantigen. PMID: 18523312
  • Our findings suggest a potential role of CMV in regulation of autoantibodies to snRNPs PMID: 19232124
  • The novel association of anti-thyroid antibodies with anti-U1RNP antibodies in juvenile onset Systemic Lupus Erythematosus seems to identify a subgroup of patients with less life-threatening organ involvement. PMID: 19419839
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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