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Mouse Anti-AHSA1 Recombinant Antibody (V2-611053) (CBMAB-A0206-LY)

The product is antibody recognizes AHSA1. The antibody 1A2-A8 immunoassay techniques such as: WB, ELISA.
See all AHSA1 antibodies
Published Data
Mouse Anti-AHSA1 Recombinant Antibody (4H9-D7) (CBMAB-A0206-LY) in IP
ΔF508-CFBE cells were transfected with CAL specific siRNA for 48 hours. Lysates were collected and used in co-immunoprecipitation experiments with A/G beads and CFTR specific antibody M3A7 (to pulldown ΔF508 CFTR). Samples from the co-immunoprecipitation fraction (left panel) and from the total lysate fraction (right panel) were assessed by western blot (5 individual experiments). Membranes were probed with antibodies against CFTR, HSP90, VCP, HSP40, HSP90, Aha1, CAL, and Ezrin (loading control). CAL knockdown is visible in total lysate. ...View More
Bergbower, E., Boinot, C., Sabirzhanova, I., Guggino, W., & Cebotaru, L. (2018). The CFTR-associated ligand arrests the trafficking of the mutant ΔF508 CFTR channel in the ER contributing to cystic fibrosis. Cellular Physiology and Biochemistry, 45(2), 639-655.
Mouse Anti-AHSA1 Recombinant Antibody (4H9-D7) (CBMAB-A0206-LY) in WB
Western blots of AHA1 levels in the cerebellar extracts from intact or ovariectimized female rats administered either saline or Δ9-THC during adolescence. The cerebellar extracts (20 μg/lane) were separated by 10% SDS-PAGE, transferred onto PDVF membranes, and subjected to western-blotting with specific antibodies. The data were quantified using a Fuji Film luminescent image analyzer (LAS-1000 Plus) and the Image Gauge program. ...View More
Filipeanu, C. M., Guidry, J. J., Leonard, S. T., & Winsauer, P. J. (2011). Δ9-THC increases endogenous AHA1 expression in rat cerebellum and may modulate CB1 receptor function during chronic use. Journal of neurochemistry, 118(6), 1101-1112.
Mouse Anti-AHSA1 Recombinant Antibody (4H9-D7) (CBMAB-A0206-LY) in ICC
Motor neurons had modest endogenous expression of Aha1 that was both cytoplasmic and nuclear. A few motor neurons were observed with cytoplasmic expression only (not shown). Heat shock had no effect on Aha1 expression in motor neurons (not shown). ...View More
Taylor, D. M., Tradewell, M. L., Minotti, S., & Durham, H. D. (2007). Characterizing the role of Hsp90 in production of heat shock proteins in motor neurons reveals a suppressive effect of wild-type Hsf1. Cell stress & chaperones, 12(2), 151.
Fig.4 Effects of chronic 9-THC and hormone status on the endogenous levels of CB1R, AHA1, and HSP90β in the striatum.
...View More
Fig.5 The effects of AHA1 over-expression on the subcellular localization of CB1R and CB2R in HEK293T cells.
...View More

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-611053
Antibody Isotype
IgG1, κ
Application
WB, ELISA

Basic Information

Immunogen
AHSA1 (AAH00321, 1 a.a. ~ 338 a.a) full-length recombinant protein with GST tag.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Preservative
None
Concentration
Batch dependent
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Activator Of HSP90 ATPase Activity 1
Entrez Gene ID
10598
UniProt ID
O95433
Alternative Names
AHA1; C14orf3; p38
Function
Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
Biological Process
Positive regulation of ATPase activity
Protein folding
Viral process
Cellular Location
Cytosol; Endoplasmic reticulum. May transiently interact with the endoplasmic reticulum.
PTM
Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.
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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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