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Linscott's Directory of Immunological & Biological Reagents
NOVUS BIOLOGICALS, LLC
 (http://www.novusbio.com)

NOVUS BIOLOGICALS, LLC

8100 Southpark Way, A-8

Littleton CO 80120

Phone: 303-730-1950

Fax: 303-730-1966

Email: novus@novusbio.com

Website: http://www.novusbio.com

 

EUROPEAN OFFICE:
Novus Biologicals, Ltd
Phone: +44 (0)1223 426001
Fax: +44 (0)871 971 1635
Email: europe@novusbio.com
Address: 12 Cambridge Science Park
Cambridge CB4 0FQ, United Kingdom

 

CANADIAN OFFICE:
Novus Biologicals Canada ULC
Phone: 855-668-8722 (855-NOVUS-CA)
Fax: 905-827-6402
Email: canada@novusbio.com
Address: 461 North Service Road West
Unit B37
Oakville, ON L6M 2V5 Canada

 
Anti-ABCB10 Polyclonal Antibody from NOVUS BIOLOGICALS, LLC

Anti-ABCB10 Polyclonal Antibody from NOVUS BIOLOGICALS, LLC

Antigenic Specificity ABCB10
Clone polyclonal
Host Species Rabbit
Reactive Species human, chimpanzee
Isotype n/a
Format immunogen affinity purified
Size 100ug, 1.08 mg/ml
Applications This antibody has been tested for use in ELISA and western blotting. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately 38-40 kDa in size corresponding to AHA1 protein. ELISA 1:35000 - 1:185000, Western Blot 1:500 - 1:3000
Description Immunogen: This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to an internal region of human AHA1 protein.. This affinity purified antibody is directed against human AHA1 protein.. Activator of Hsp90 ATPase (AHA1) stimulates the inherent ATPase cycle of Hsp90, which is essential for its chaperone activity in vivo. The activation and/or stability of many of the key regulatory and signaling proteins of the eukaryotic cell depend on their interaction with the Hsp90 molecular chaperone. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series both to assist client-protein recruitment or release and to modulate progress through the ATPase coupled chaperone cycle. Structural analysis and mutagenesis show that binding of the N-terminal domain of AHA1 to Hsp90 promotes a conformational switch in the middle-segment catalytic loop (aa 370y390) of Hsp90 that exposes the catalytic Arg380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone. Recent studies show that AHA1 modulates Hsp90-dependent stability of the folding of the cystic fibrosis transmembrane conductance regulator (CFTR) in the endoplasmic reticulum (ER). Down-regulation of AHA1 rescues misfolding of CFTR in cystic fibrosis.
Catalog # NBP1-77943
Price $325.00
Other Names Abcb10
Supplier Data Page Anti-ABCB10 from NOVUS BIOLOGICALS, LLC
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