Recombinant Human Gem-associated protein 2 (GEMIN2)

Code CSB-YP021329HU
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Source Yeast
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Code CSB-EP021329HU
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Source E.coli
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Code CSB-EP021329HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP021329HU
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Source Baculovirus
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Code CSB-MP021329HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
GEMIN2
Uniprot No.
Alternative Names
Component of gems 2; Gem (nuclear organelle) associated protein 2; Gem associated protein 2; GEMI2_HUMAN; Gemin-2; gemin2; SIP 1; SIP-1; SIP1; SIP1 delta; SIP1-delta; SMN interacting protein 1; SMN interacting protein 1 delta; SMN-interacting protein 1; Survival interacting protein 1; Survival of motor neuron protein interacting protein 1; Survival of motor neuron protein-interacting protein 1
Species
Homo sapiens (Human)
Expression Region
1-280
Target Protein Sequence
MRRAELAGLK TMAWVPAESA VEELMPRLLP VEPCDLTEGF DPSVPPRTPQ EYLRRVQIEA AQCPDVVVAQ IDPKKLKRKQ SVNISLSGCQ PAPEGYSPTL QWQQQQVAQF STVRQNVNKH RSHWKSQQLD SNVTMPKSED EEGWKKFCLG EKLCADGAVG PATNESPGID YVQIGFPPLL SIVSRMNQAT VTSVLEYLSN WFGERDFTPE LGRWLYALLA CLEKPLLPEA HSLIRQLARR CSEVRLLVDS KDDERVPALN LLICLVSRYF DQRDLADEPS
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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 -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound.
Gene References into Functions
  1. Specific mutations in the yeast Sm protein ring expose a requirement for assembly factor Brr1, a homolog of human Gemin2. PMID: 27974620
  2. The authors propose that Gemin2 is a versatile hub for ribonucleoprotein exchange that functions broadly in RNA metabolism. PMID: 26828962
  3. investigate the oligomeric nature of the SMN.Gemin2 complexes from humans and fission yeast (hSMN.Gemin2 and ySMN.Gemin2) PMID: 26092730
  4. Two monoclonal antibodies against SMN (survival-of-motor-neurons) protein bind to its site of interaction with gemin2. PMID: 23939045
  5. 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. PMID: 22607171
  6. 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 PMID: 21913013
  7. purified SMN-GEMIN2 fusion protein enhanced the RAD51-mediated homologous pairing much more efficiently than GEMIN2 alone PMID: 21732698
  8. 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. PMID: 21816274
  9. Novel monoclonal antibodies detect SIP1 in the cytoplasm of human cells from multiple tumor tissue arrays. PMID: 20515682
  10. 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. PMID: 19830559
  11. This study supports the rationale for developing SIP1 as a potential therapeutic and diagnostic target for gliomas PMID: 19806322
  12. 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 PMID: 19915660
  13. Spinal muscular atrophy and amyotropic lateral sclerosis patients have decreased SIP 1-alpha and increased SIP 1-beta expression levels compared to normal tissues. PMID: 11943600
  14. SIP1 determines the capacity for snRNP assembly: biochemical deficiency in spinal muscular atrophy. PMID: 15964810
  15. binds to HIV-1 integrase and facilitates viral cDNA synthesis and subsequent steps that precede integration in vivo PMID: 16731905
  16. 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 PMID: 17308308
  17. relationship between the feature of gene mutations and single nucleotide polymorphisms of SIP1 gene and HSCR PMID: 18247312
  18. We found upregulation of mRNA for transcription factors Snail, Slug, Twist, and SIP1 in spindle cell carcinoma when compared to squamous cell carcinoma. PMID: 19381684

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Subcellular Location
Nucleus, gem. Cytoplasm. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs. Also found in the cytoplasm.
Protein Families
Gemin-2 family
Database Links

HGNC: 10884

OMIM: 602595

KEGG: hsa:8487

STRING: 9606.ENSP00000308533

UniGene: Hs.652307

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