The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions.
The presence of the J domain defines a protein as a member of the DnaJ family.
DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein.
The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis.
The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function.
DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis.
DnaJB2 (DnaJ homolog subfamily B member 2), also known as HSJ1 or HSPF3, is expressed almost exclusively in the brain, with the highest levels in the frontal cortex and hippocampus.
Two isoforms are produced due to alternative splicing.
Applications:Suitable for use in ELISA and Western Blot.
Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for 12 months after receipt.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：50ul
Host：rabbit
Source Antibody：human
Grade：Affinity Purified
Purity：Purified by immunoaffinity chromatography.
Form：Supplied as a liquid in PBS, pH 7.3, 0.09% sodium azide, 50% glycerol.
Specificity：Recognizes human DNAJB2. Species Crossreactivity: mouse and rat
