HNRNPA1, CT (HNRNPA1, HNRPA1, Heterogeneous nuclear ribonucleoprotein A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1) (Azide free) (HRP)

Referência 036658-HRP-200ul

Tamanho : 200ul

Marca : US Biological

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036658-HRP HNRNPA1, CT (HNRNPA1, HNRPA1, Heterogeneous nuclear ribonucleoprotein A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1) (Azide free) (HRP) discontinued

Clone Type
Polyclonal
Host
rabbit
Source
human
Swiss Prot
P09651
Isotype
IgG
Grade
Affinity Purified
Applications
E WB
Crossreactivity
Hu
Accession #
NP_002127.1; NP_112420.1
Gene #
HNRNPA1
Shipping Temp
Blue Ice
Storage Temp
-20°C

This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It is one of the most abundant core proteins of hnRNP complexes and it is localized to the nucleoplasm. This protein, along with other hnRNP proteins, is exported from the nucleus, probably bound to mRNA, and is immediately re-imported. Its M9 domain acts as both a nuclear localization and nuclear export signal. The encoded protein is involved in the packaging of pre-mRNA into hnRNP particles, transport of poly A+ mRNA from the nucleus to the cytoplasm, and may modulate splice site selection. It is also thought have a primary role in the formation of specific myometrial protein species in parturition. Multiple alternatively spliced transcript variants have been found for this gene but only two transcripts are fully described. These variants have multiple alternative transcription initiation sites and multiple polyA sites. [provided by RefSeq].||Applications:|Suitable for use in Western Blot and ELISA. Other applications not tested.||Recommended Dilution:|Optimal dilutions to be determined by the researcher.||Storage and Stability:|Store product at 4°C if to be used immediately within two weeks. For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C. Aliquots are stable at -20°C for 12 months after receipt. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Note: Sodium azide is a potent inhibitor of peroxidase and should not be added to HRP conjugates. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. ||Note: Applications are based on unconjugated antibody.

Applications
Product Type: Pab|Isotype: IgG|Host: rabbit|Source: human|Concentration: As Reported|Form: Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with horseradish peroxidase (HRP).|Purity: Purified by Protein A and peptide affinity chromatography. |Immunogen: KLH-conjugated synthetic peptide mapping to a fragment of residues within amino acids 266-294 from the C-terminal region of human HNRNPA1.|Specificity: Recognizes human HNRNPA1.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Immunogen
KLH-conjugated synthetic peptide mapping to a fragment of residues within amino acids 266-294 from the C-terminal region of human HNRNPA1.
Form
Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with horseradish peroxidase (HRP).
Purity
Purified by Protein A and peptide affinity chromatography.
Specificity
Recognizes human HNRNPA1.
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)|Michlewski, G., et al. Nat. Struct. Mol. Biol. 17(8):1011-1018(2010)|Clower, C.V., et al. Proc. Natl. Acad. Sci. U.S.A. 107(5):1894-1899(2010)|David, C.J., et al. Nature 463(7279):364-368(2010)|Fisette, J.F., et al. RNA 16(1):228-238(2010)