Human Heat Shock Protein 90 kDa Alpha A1 (HSP90aA1) Protein

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195€ (10 µg)

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935106861
info@markelab.com
name
Human Heat Shock Protein 90 kDa Alpha A1 (HSP90aA1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx067017
tested applications
WB, SDS-PAGE

Description

Human Heat Shock Protein 90kDa Alpha A1 (HSP90aA1) is a recombinant Human protein expressed in E. coli.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Heat Shock Protein 90 kDa Alpha A1 (HSP90aA1)
Host
E. coli
Assay Type
Activity: Not tested
Sequence Fragment: Met1-Gly496 linked with Ile698-Asp732
Tag: N-terminal His tag
Origin
Human
Conjugation
Unconjugated
Observed MW
Calculated MW: 62.9 kDa  Observed MW (SDS-PAGE): 72 kDa
Expression
Recombinant
Purity
> 95%
Size 1
10 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
500 µg
Form
Lyophilized
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 1 mM EDTA, 1 mM DTT, 0.01% Sarcosyl, 5% Trehalose and Proclin-300.
Availability
Shipped within 5-7 working days.
Storage
Store lyophilized form at 2-8°C for up to 1 month. For longer periods, store lyophilized or liquid at -80°C. Avoid repeated freeze–thaw cycles.
Dry Ice
No
UniProt ID
P07900
Background
Protein HSP90aA1
Status
RUO
Note
THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.
To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in 20 mM Tris, 150 mM NaCl, pH 8.0. If a higher concentration is required, the product can be reconstituted directly in 20 mM Tris, 150 mM NaCl, pH 8.0, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Concentration: Prior to lyophilization: 200 µg/ml

Descripción

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