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Mouse (Murine) Monoclonal GEMIN2 Primary Antibody for ICC, FACS - ABIN108541
Liu, Fischer, Wang, Dreyfuss: The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. in Cell 1997
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Mouse (Murine) Monoclonal GEMIN2 Primary Antibody for ICC, FACS - ABIN108540
Takizawa, Qing, Takaku, Ishida, Morozumi, Tsujita, Kogame, Hirota, Takahashi, Shibata, Kurumizaka, Takeda: GEMIN2 promotes accumulation of RAD51 at double-strand breaks in homologous recombination. in Nucleic acids research 2010
Show all 8 Pubmed References
Human Monoclonal GEMIN2 Primary Antibody for IF, IP - ABIN2668496
Oztas, Avci, Ozcan, Sayan, Tulchinsky, Yagci: Novel monoclonal antibodies detect Smad-interacting protein 1 (SIP1) in the cytoplasm of human cells from multiple tumor tissue arrays. in Experimental and molecular pathology 2010
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Specific mutations in the yeast Sm protein ring expose a requirement for assembly factor Brr1, a homolog of human Gemin2.
The authors propose that Gemin2 is a versatile hub for ribonucleoprotein exchange that functions broadly in RNA metabolism.
investigate the oligomeric nature of the SMN.Gemin2 complexes from humans and fission yeast (hSMN.Gemin2 and ySMN.Gemin2)
Two monoclonal antibodies against SMN (survival-of-motor-neurons) protein bind to its site of interaction with gemin2.
several conserved SMN residues, including the sites of two SMA patient mutations, are not required for binding to Gemin2. Instead, they form a conserved SMN/Gemin2 surface that may be functionally important for snRNP assembly.
Overexpression of SIP1 and downregulation of E-cadherin is associated with delayed neck metastasis in stage I/II oral tongue squamous cell carcinoma after partial glossectomy
purified SMN-GEMIN2 fusion protein enhanced the RAD51-mediated homologous pairing much more efficiently than GEMIN2 alone
Study identified Gemin2 as the protein that binds a pentamer of Sm proteins comprised of SmD1/D2 and SmF/E/G; the crystal structure of this complex bound to SMN's Gemin2 binding domain to 2.5 A was determined.
Novel monoclonal antibodies detect SIP1 in the cytoplasm of human cells from multiple tumor tissue arrays.
This study demonstrated that miR-141 levels correlate inversely with SIP1 protein levels as well as cell migration and invasion of CRC cells; SIP1 was identified as a functional target of miR-141.
This study supports the rationale for developing SIP1 as a potential therapeutic and diagnostic target for gliomas
SIP1 appears to stabilize functional multimer forms of IN, thereby promoting the assembly of IN and RT on viral RNA to allow efficient reverse transcription, which is a prerequisite for efficient HIV-1 infection
Spinal muscular atrophy and amyotropic lateral sclerosis patients have decreased SIP 1-alpha and increased SIP 1-beta expression levels compared to normal tissues.
SIP1 determines the capacity for snRNP assembly: biochemical deficiency in spinal muscular atrophy.
binds to HIV-1 integrase and facilitates viral cDNA synthesis and subsequent steps that precede integration in vivo
Gemin2 plays an important role in small nuclear ribonucleoprotein assembly through the stabilization of the survival of motor neuron oligomer/complex via novel self-interaction
relationship between the feature of gene mutations and single nucleotide polymorphisms of SIP1 gene and HSCR
We found upregulation of mRNA for transcription factors Snail, Slug, Twist, and SIP1 in spindle cell carcinoma when compared to squamous cell carcinoma.
utilised a targeted screen to identify mRNA associated with SMN, Gemin2 and Gemin3 in the cytoplasm of a human neuroblastoma cell line, SHSY5Y
Gene targeting in mice reveals a correlation between defects in the biogenesis of U snRNPs and motoneuron cell death (gemin2; SMN interacting protein 1)
Reduction of Gemin2, unlike reduction of SMN, in zebrafish embryos does not directly cause motor axon outgrowth defects.
This gene encodes one of the proteins found in the SMN complex, which consists of several gemin proteins and the protein known as the survival of motor neuron protein. The SMN complex is localized to a subnuclear compartment called gems (gemini of coiled bodies) and is required for assembly of spliceosomal snRNPs and for pre-mRNA splicing. This protein interacts directly with the survival of motor neuron protein and it is required for formation of the SMN complex. A knockout mouse targeting the mouse homolog of this gene exhibited disrupted snRNP assembly and motor neuron degeneration.
SMN interacting protein 1-delta
, component of gems 2
, gem-associated protein 2
, survival of motor neuron protein interacting protein 1
, SMN-interacting protein 1
, survival of motor neuron protein-interacting protein 1
, survivor of motor neuron protein interacting protein 1
, SMN interacting protein-1
, Survival of motor neuron protein-interacting protein 1