Product Name: HNRNPH1 Antibody
Species Reactivity: Human
Tested Applications: WB
Applications: For WB starting dilution is: 1:1000
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 49 kDa
Immunogen: This HNRNPH1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 48-77 amino acids from the N-terminal region of human HNRNPH1.
Host Species: Rabbit
Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.
Physical State: Liquid
CAS NO.: 1825355-56-3
Product: AZD3839 (free base)
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: 0.5 mg/ml
Storage Conditions: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: Heterogeneous nuclear ribonucleoprotein H, hnRNP H, Heterogeneous nuclear ribonucleoprotein H, N-terminally processed, HNRNPH1, HNRPH, HNRPH1
Accession NO.: P31943
Protein Ino: 1710632
Official Symbol: HNRNPH1
Geneid: 3187
Background: This gene belongs to the subfamily of ubiquitouslyexpressed heterogeneous nuclear ribonucleoproteins (hnRNPs). ThehnRNPs are RNA binding proteins and they complex with heterogeneousnuclear RNA (hnRNA). These proteins are associated with pre-mRNAsin the nucleus and appear to influence pre-mRNA processing andother aspects of mRNA metabolism and transport. While all of thehnRNPs are present in the nucleus, some seem to shuttle between thenucleus and the cytoplasm. The hnRNP proteins have distinct nucleicacid binding properties. The protein encoded by this gene has threerepeats of quasi-RRM domains that bind to RNAs. It is very similarto the family member HNRPF. This gene is thought to be potentiallyinvolved in hereditary lymphedema type I phenotype. [provided byRefSeq].
PubMed ID:http://aac.asm.org/content/23/3/407.abstract