TNPO3 Antibody, Biotin conjugated

Code CSB-PA757558LD01HU
Size US$166
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) TNPO3 Polyclonal antibody
Uniprot No.
Target Names
TNPO3
Alternative Names
ibody; Imp12 antibody; Importin 12 antibody; Importin-12 antibody; IPO12 antibody; MTR10A antibody; TNPO3 antibody; TNPO3_HUMAN antibody; Transportin 3 antibody; Transportin SR antibody; Transportin-3 antibody; Transportin-SR antibody; TRN SR antibody; TRN-SR antibody; TRN-SR2 antibody; TRNSR antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Transportin-3 protein (382-458AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Biotin
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Importin, which transports target proteins into the nucleus. Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains. Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation. The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively. Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus.; (Microbial infection) Involved in immunodeficiency virus (HIV-1) infection by importing the pre-integration complex (PIC) into the nucleus. Required for a nuclear maturation step of HIV-1 prior to integration.
Gene References into Functions
  1. Combining these results with small-angle X-ray scattering data for the complex of TRN-SR2 with truncated integrase, we propose a molecular model of the complex. We speculate that nuclear import of the PIC may proceed concurrently with the normal nuclear transport. PMID: 28356354
  2. IRF5-TNPO3 genetic variation is associated systemic lupus erythematosus. PMID: 25205108
  3. Data suggest that the HIV-1 integrase (IN)/transportin-SR2 (TRN-SR2) interaction interface is a potential target for antiviral therapy. PMID: 25063804
  4. Tnpo3 mutants that are not able to interact with cleavage and polyadenylation specificity factor 6 do not facilitate HIV-1 infectivity, suggesting a potential route of pharmacological intervention in the treatment of AIDS. PMID: 24449914
  5. TNPO3 mutation is the cause of limb-girdle muscular dystrophy 1F, expands knowledge of the molecular basis of muscular dystrophies and bolsters the importance of defects of nuclear envelope proteins as causes of inherited myopathies. PMID: 23543484
  6. The TNPO3 gene is mapped within the Limb-girdle muscular dystrophy 1F critical interval and its 923-amino acid human gene product is also expressed in skeletal muscle. PMID: 23667635
  7. a model wherein one monomer of TRN-SR2 is bound to one monomer of RanGTP. PMID: 23878195
  8. In skeletal muscle of limb-girdle muscular dystrophy 1F individuals, expression of transportin 3 indicates altered transportin 3 function. PMID: 23543484
  9. These results suggest that TNPO3 and cyclophilin A facilitate HIV-1 infection by coordinating proper uncoating of the core in target cells. PMID: 23097435
  10. Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein. PMID: 22872638
  11. TNPO3 can directly engage the HIV-1 IN tetramer prebound to the cognate DNA. PMID: 22872640
  12. Transportin 3 and importin alpha act as receptors and are required for effective nuclear import of HIV-1 integrase in virus-infected cells. PMID: 21326825
  13. TNPO3 interacts with HIV-1 gag in the cytoplasm to assist HIV-1 infection after nuclear import. PMID: 22398280
  14. TNPO3 promotes HIV-1 infectivity at a step in the virus life cycle that is detectable after the preintegration complex arrives in the nucleus and capsid is the viral determinant for TNPO3 dependence. PMID: 22145813
  15. TNPO3 binds to a surface of monomeric HIV-1 integrase that remains exposed after tetramerization. PMID: 22176773
  16. a novel nuclear localization signal and mechanism for serpinF1 nuclear import PMID: 22028839
  17. The authors demonstrated that TNPO3 was required by several lentiviruses for nuclear import. PMID: 21976643
  18. Tnp3 binds to tRNAs and capsids proteins, and is required for efficient HIV-1 integration. PMID: 21901095
  19. Here the authors discover a link between the viral entry of HIV and its interaction with TRN-SR2. PMID: 21276267
  20. capsid, not integrase, is the dominant viral factor that dictates transportin 3 dependency during HIV-1 infection PMID: 19846519
  21. Results imply that the mechanism by which SR proteins are imported to the nucleus is conserved between Drosophila and humans and involves the nuclear import receptor transportin-SR PMID: 12134081

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Involvement in disease
Limb-girdle muscular dystrophy 1F (LGMD1F)
Subcellular Location
Nucleus envelope. Cytoplasm.
Tissue Specificity
Expressed in skeletal muscle.
Database Links

HGNC: 17103

OMIM: 608423

KEGG: hsa:23534

STRING: 9606.ENSP00000265388

UniGene: Hs.193613

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