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DNAJA4 Polyclonal Antibody Reactivity Human

SKU: E-AB-53105-200

  • $ 55995
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DNAJA4 Polyclonal Antibody Reactivity Human

 

SKU # E-AB-53105
Reactivity Human, Mouse
Host Rabbit
Applications WB, IHC

 

Product Details

Isotype IgG
Host Rabbit
Reactivity Human, Mouse
Applications WB, IHC
Clonality Polyclonal
Immunogen Fusion protein of human DNAJA4
Abbre DNAJA4
Synonyms member4,   subfamily A,  DNAJ A4,  DNAJA 4,  DNAJA4,  DNJA4,  DnaJ (Hsp40) homolog,  DnaJ (Hsp40) homolog subfamily A member 4,  DnaJ heat shock protein family (Hsp40) member A4,  DnaJ homolog subfamily A member 4,  MST104,  MSTP104,  PRO1472
Swissprot
Calculated MW 45 kDa
Observed MW Refer to figures
Cellular Localization Membrane.
Concentration 0.84 mg/mL
Buffer Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol.
Purification Method Antigen affinity purification
Research Areas Cancer,  Cardiovascular,  Metabolism,  Signal transduction
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended.

 

Related Reagents

Applications Recommended Dilution
WB 1:500-1:2000
IHC 1:50-1:200

 

Background

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. DnaJA4 (DnaJ homolog subfamily A member 4) is a SREBP-regulated chaperone that is thought to regulate the cholesterol biosynthesis pathway.