Human Serine/Threonine-Protein Phosphatase 2B Catalytic Subunit Alpha Isoform (PPP3CA) Protein

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234€ (10 µg)

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935106861
info@markelab.com
name
Human Serine/Threonine-Protein Phosphatase 2B Catalytic Subunit Alpha Isoform (PPP3CA) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx065654
tested applications
WB, SDS-PAGE

Description

Recombinant Serine/Threonine-Protein Phosphatase 2B Catalytic Subunit Alpha Isoform (PPP3CA) is a recombinant Human protein produced in a Prokaryotic expression system (E. coli).

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Proteins and Peptides
Immunogen Target
Serine/Threonine-Protein Phosphatase 2B Catalytic Subunit Alpha Isoform (PPP3CA)
Host
E. coli
Origin
Human
Conjugation
Unconjugated
Observed MW
Molecular Weight: Calculated MW: 37.4 kDa  Observed MW (SDS-PAGE): 39 kDa

Concentration: Prior to lyophilization: 200 µg/ml

Sequence Fragment: Ile7-Ser301

Tag: N-terminal His tag
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 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 PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, 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.
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Availability
Shipped within 5-7 working days.
Storage
Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
Q08209
Background
Protein PPP3CA
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

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