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Cell Signaling Hsp90alpha (D1a7) Rabbit mAb
List Price
$354.51
Your Price
$354.51
Cell Signaling Hsp90alpha (D1a7) Rabbit mAb - CSIG (Additional S&H or Hazmat Fees May Apply)
NETA PART:
CSIG-8165S
MFG.PART:
8165S
UNSPSC:
12352203
Manufacturer:
Cell Signaling
| Size | 100 µl |
| Reactivity | H R Hm Mk B Pg |
| Sensitivity | Endogenous |
| Molecular Weight (kDa) | 90 |
| Source/Isotype | Rabbit IgG |
| Application/Dilution | {Western Blotting: 1:1000} |
| Storage | Supplied in 10 mm sodium HEPES (pH 7.5), 150 mm NaCl, 100 µg/mL BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody. |
| Specificity/Sensitivity | HSP90α (D1A7) Rabbit mAb recognizes endogenous levels of total HSP90α protein. This antibody does not cross-react with HSP90β or other heat shock proteins. |
| Species Reactivity | Human, Rat, Hamster, Monkey, Bovine, Pig |
| Source/Purification | Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu80 of human HSP90α protein. |
| Background | HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2). |
| SKU | CSIG-8165S |
|---|---|
| Supplier Part Number | 8165S |
| UM | EA |
| UNSPSC | 12352203 |
| Manufacturer Name | Cell Signaling |
| MSDS URL | Click here |
| Temperature | -20C |
| CountryOfOrigin | United States |
| ProductLine | CSIG |
| Qty | 1 |
| MinOrderQty | 1 |
| Weight | 7.000000 |
| Lead Time | 5 |
| Hazardous | N |
| Energy Star | No |
| Green | No |
| Controlled | N |