Datasheet

HSP90 alpha protein-HIS Epitope

Name: HSP90 alpha protein-HIS Epitope
Brand: Rockland Immunochemicals
Price: 325.0 USD
Availability: OutOfStock

Item No. 009-001-F69

Size: 50 µg

Physical State: Liquid (sterile filtered)

Origin: Human

Expressed in: Sf9 cells

$665.00 /Per Item

20 µg $325.00

50 µg $665.00

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Specifications for HSP90 alpha protein-HIS Epitope

Product Details

Description: HSP90 alpha recombinant protein-HIS Epitope - 009-001-F69

Synonyms: HSP90AA1, HSPN, LAP2, HSP86, HSPC1, HSPCA, Hsp89, Hsp90, HSP90N, HSPCAL1, HSPCAL4, FLJ31884, Heat shock protein HSP 90-alpha, Heat shock 86 kDa, HSP 86, HSP86, Lipopolysaccharide-associated protein 2, LAP-2, LPS-associated protein 2, Renal carcinoma antigen NY-REN-38

Species of Origin: Human

Expressed in: Sf9 cells

Type: Recombinant Protein

Target Details

Gene Name: HSPA90AA1 - View All HSPA90AA1 Products

Purity/Specificity: Recombinant full length human HSP90α was expressed by baculovirus in Sf9 insect cells using a C-Terminal his epitope. The purity was determined to be >85% by densitometry.

Database Links:

P07900 - UniProtKB

NP_001017963.2 - NCBI Protein

?term=NM_005348 - Gene ID

Application Details

Application Note: HSP90α Protein is stored in 50mM Sodium Phosphate, pH: 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 2mM DTT, 25% glycerol. HSP90α Protein is suitable for use in Western Blot. Expect a band approximately ~94kDa on specific lysates or tissues. Specific conditions for reactivity should be optimized by the end user.

Formulation

Concentration: 0.1 µg/µL

Buffer: See application note.

Shipping & Handling

Shipping Condition: Dry Ice

Storage Condition: Store product at –70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Expiration: Expiration date is one (1) year from date of receipt.

Background

HSP90α is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins (1). HSP90 is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including HER2/ERBB2, AKT, RAF1, BCR-ABL and mutated p53. HSP90 inhibitors bind to HSP90, and induce the proteasomal degradation of HSP90 client proteins. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (2). HSP90α Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, and Cellular Stress research.

Certificate of Analysis Lookup

Disclaimer

This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.