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Rabbit Anti-eIF2C2/Gold Conjugated antibody (bs-12450R-Gold)
訂購熱線:400-901-9800
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說 明 書: 100ul(10nm  15nm  35nm
100ul/2980.00元
大包裝/詢價
產(chǎn)品編號 bs-12450R-Gold
英文名稱 Rabbit Anti-eIF2C2/Gold Conjugated antibody
中文名稱 膠體金標(biāo)記的真核翻譯起始因子2C2抗體
別    名 Ago 2; AGO2_HUMAN; Argonaute 2; Argonaute2; dAgo2; eIF 2C 2; eIF-2C 2; eIF2C 2; Eif2c2; Eukaryotic translation initiation factor 2C 2; hAgo2; MGC3183; PAZ Piwi domain protein; PPD; Protein argonaute-2; Protein slicer; Q10; Slicer protein.   
規(guī)格價格 100ul/2980元 購買        大包裝/詢價
說 明 書 100ul(10nm  15nm  35nm
研究領(lǐng)域 細(xì)胞生物  染色質(zhì)和核信號  表觀遺傳學(xué)  
抗體來源 Rabbit
克隆類型 Polyclonal
交叉反應(yīng) (predicted: Human, Mouse, Rat, Dog, Pig, Cow, Horse, Sheep, )
產(chǎn)品應(yīng)用 IEM=1:20-200 ICA=1:20-200 ChIP=1:20-200 
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量 97kDa
性    狀 Lyophilized or Liquid
濃    度 0.4mg/ml
免 疫 原 KLH conjugated synthetic peptide derived from human eIF2C2/Ago2
亞    型 IgG
純化方法 affinity purified by Protein A
儲 存 液 0.02M TBS(pH8.2) with 1% BSA, 0.03% Proclin300.
保存條件 Store at 2-8 oC for 3-6 months. Avoid repeated freeze/thaw cycles.
產(chǎn)品介紹 background:
Eukaryotic translation initiation factor 2C (eIF2C) proteins (argonaute family) influence RNA interference (RNAi) as components of the RNA-inducible silencing complex (RISC) or microRNA (miRNA)-containing ribonucleoprotein particle (miRNP). Small RNAs, including small interfering RNAs (siRNAs) and miRNAs, can silence target genes through mechanisms that utilize RISC or miRNP particles. eIF2C1 (argonaute 1, AGO1, eIF2C, GERP95, Q99) and Dicer1 play a coordinated role in siRNA-mediated gene silencing. eIF2C2 (Slicer, argonaute 2, AGO2, Q10) is a RISC component that can concentrate in cytoplasmic processing bodies (P-bodies) and catalyze mRNA cleavage. Mammalian P-bodies contain mRNAs and have an association with miRNA-induced translational silencing and siRNA-induced mRNA degradation. Additional eIF2C proteins include eIF2C3 (argonaute 3, AGO3), eIF2C4 (argonaute 4, AGO4) and meIF2c5 (mouse argonaute 5).

Function:
Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include EIF2C2/AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by EIF2C2/AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also upregulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and upregulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions.

Subunit:
Interacts with DICER1 through its Piwi domain and with TARBP2 during assembly of the RNA-induced silencing complex (RISC). Together, DICER1, EIF2C2/AGO2 and TARBP2 constitute the trimeric RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto EIF2C2/AGO2. EIF2C2/AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Note however that the term RISC has also been used to describe the trimeric RLC/miRLC. The formation of RISC complexes containing siRNAs rather than miRNAs appears to occur independently of DICER1. Interacts with EIF2C1/AGO1. Also interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9, EIF6, ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10, PABPC1, PRMT5, P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with the P-body components DCP1A and XRN1. Associates with polysomes and messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the interaction is modulated under stress-induced conditions, occurs under both cell proliferation and differentiation conditions and in a RNA-and phosphorylation-independent manner. Interacts with LIMD1, WTIP and AJUBA. Interacts with TRIM71.

Subcellular Location:
Cytoplasm > P-body. Nucleus. Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8.

Post-translational modifications:
Hydroxylated. 4-hydroxylation appears to enhance protein stability but is not required for miRNA-binding or endonuclease activity.

Similarity:
Belongs to the argonaute family. Ago subfamily.
Contains 1 PAZ domain.
Contains 1 Piwi domain.

Database links:

Entrez Gene: 27161 Human

Entrez Gene: 239528 Mouse

Entrez Gene: 59117 Rat

Omim: 606229 Human

SwissProt: Q9UKV8 Human

SwissProt: Q8CJG0 Mouse

SwissProt: Q9QZ81 Rat

Unigene: 449415 Human

Unigene: 475937 Mouse

Unigene: 35512 Rat



Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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