TARDBP Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application
| IHC-P, IF, WB, E |
|---|---|
| Primary Accession | Q13148 |
| Other Accession | Q921F2, Q5ZLN5, NP_031401.1 |
| Reactivity | Human, Rat, Mouse |
| Predicted | Chicken, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 44740 Da |
| Antigen Region | 1-30 aa |
| Gene ID | 23435 |
|---|---|
| Other Names | TAR DNA-binding protein 43, TDP-43, TARDBP, TDP43 |
| Target/Specificity | This TARDBP antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human TARDBP. |
| Dilution | IHC-P~~1:100 IF~~1:10~50 WB~~1:2000 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.05% (V/V) Proclin 300. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | TARDBP Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TARDBP {ECO:0000303|PubMed:18396105, ECO:0000312|HGNC:HGNC:11571} |
|---|---|
| Function | RNA-binding protein that is involved in various steps of RNA biogenesis and processing (PubMed:23519609). Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases (PubMed:21358640, PubMed:29438978). Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts (PubMed:28794432). Also regulates mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening (PubMed:30520513). In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival (PubMed:19765185, PubMed:23398327). Also participates in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively regulates the expression of CDK6 (PubMed:19760257). Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner (PubMed:25678563). |
| Cellular Location | Nucleus. Cytoplasm. Cytoplasm, Stress granule Mitochondrion. Note=Continuously travels in and out of the nucleus (PubMed:18957508). Localizes to stress granules in response to oxidative stress (PubMed:19765185). A small subset localizes in mitochondria (PubMed:28794432). |
| Tissue Location | Ubiquitously expressed. In particular, expression is high in pancreas, placenta, lung, genital tract and spleen |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, this protein regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20. [provided by RefSeq].
REFERENCES
Kim, S.H., et al. J. Biol. Chem. 285(44):34097-34105(2010)
Geser, F., et al. Arch. Neurol. 67(10):1238-1250(2010)
Mackenzie, I.R., et al. Lancet Neurol 9(10):995-1007(2010)
Shan, X., et al. Proc. Natl. Acad. Sci. U.S.A. 107(37):16325-16330(2010)
McKee, A.C., et al. J. Neuropathol. Exp. Neurol. 69(9):918-929(2010)
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