Recombinant Human CD37 protein (Fc Chimera) (ab219877)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 90% SDS-PAGE
- Endotoxin level: < 1.000 Eu/µg
- Suitable for: SDS-PAGE
Description
-
Product name
Recombinant Human CD37 protein (Fc Chimera)
See all CD37 proteins and peptides -
Purity
> 90 % SDS-PAGE. -
Endotoxin level
< 1.000 Eu/µg -
Expression system
HEK 293 cells -
Accession
-
Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
-
Species
Human -
Sequence
AQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWF QVLILRGNGSEAHRVPCSCYNLSATNDSTILDKVILPQLSRLGHLARSRH SADICAVPAESHIYREGCAQGLQKWLHN -
Predicted molecular weight
42 kDa including tags -
Amino acids
113 to 240 -
Additional sequence information
Fused with a human IgG1 Fc tag at the N-terminus (AAI06753).
-
Specifications
Our Abpromise guarantee covers the use of ab219877 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
-
Applications
SDS-PAGE
-
Form
Lyophilized -
Concentration information loading...
Preparation and Storage
-
Stability and Storage
Shipped at 4°C. Store at -80°C. Avoid freeze / thaw cycle.
pH: 7.4
Constituents: 0.61% Tris, 0.75% Glycine, 5% Trehalose
Lyophilized from 0.22 µm filtered solution.
5-10% trehalose is commonly used for freeze drying, and after reconstitution, the trehalose is mostly about 3-5% -
ReconstitutionReconstitute with sterile deionized water to a concentration of 200 µg/ml.
General Info
-
Alternative names
- CD 37
- CD37
- CD37 antigen
see all -
Tissue specificity
B-lymphocytes. -
Sequence similarities
Belongs to the tetraspanin (TM4SF) family. -
Cellular localization
Membrane. - Information by UniProt
Images
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
References (0)
ab219877 has not yet been referenced specifically in any publications.