Recombinant Human SSR2 protein (ab140550)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE, MS
Description
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Product name
Recombinant Human SSR2 protein -
Purity
> 90 % SDS-PAGE.
ab140550 is purified using conventional chromatography techniques. -
Expression system
Escherichia coli -
Accession
-
Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MGSSHHHHHH SSGLVPRGSH MGSEEGARLL ASKSLLNRYA VEGRDLTLQY NIYNVGSSAA LDVELSDDSF PPEDFGIVSG MLNVKWDRIA PASNVSHTVV LRPLKAGYFN FTSATITYLA QEDGPVVIGS TSAPGQGGIL AQREFDRRFS PHFLD -
Predicted molecular weight
17 kDa including tags -
Amino acids
18 to 149 -
Tags
His tag N-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab140550 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
Mass Spectrometry
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Mass spectrometry
MALDI-TOF -
Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 8.00
Constituents: 0.32% Tris HCl, 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride
General Info
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Alternative names
- Beta SSR
- DKFZp686F19123
- HSD25
see all -
Function
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. -
Sequence similarities
Belongs to the TRAP-beta family. -
Cellular localization
Endoplasmic reticulum membrane. - Information by UniProt
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
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SDS download
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Datasheet download
References (0)
ab140550 has not yet been referenced specifically in any publications.