Recombinant Human TMP21 protein (ab167877)
Key features and details
- Expression system: Escherichia coli
- Purity: > 85% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE, MS
Description
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Product name
Recombinant Human TMP21 protein -
Purity
> 85 % SDS-PAGE.
purified by 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 MGSISFHLPI NSRKCLREEI HKDLLVTGAY EISDQSGGAG GLRSHLKITD SAGHILYSKE DATKGKFAFT TEDYDMFEVC FESKGTGRIP DQLVILDMKH GVEAKNYEEI AKVEKLKPLE VELRRLEDLS ESIVNDFAYM KKREEEMRDT NESTNTR -
Predicted molecular weight
20 kDa including tags -
Amino acids
32 to 185 -
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 ab167877 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 buffer, 30% Glycerol (glycerin, glycerine), 0.88% Sodium chloride
General Info
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Alternative names
- 1110014C03Rik
- 21 kDa transmembrane trafficking protein
- 21 kDa transmembrane-trafficking protein
see all -
Function
Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act togther with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1 (By similarity). In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus. -
Tissue specificity
Ubiquitous. -
Sequence similarities
Belongs to the EMP24/GP25L family.
Contains 1 GOLD domain. -
Domain
The lumenal domain mediates localization to the plasma membrane by partially overriding the ER retention by the cytoplasmic domain. -
Cellular localization
Golgi apparatus > cis-Golgi network membrane. Melanosome. Endoplasmic reticulum membrane. Endoplasmic reticulum-Golgi intermediate compartment membrane. Cytoplasmic vesicle > secretory vesicle membrane. Cell membrane. Golgi apparatus > trans-Golgi network membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Cycles between compartments of the early secretatory pathway. - 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)
ab167877 has not yet been referenced specifically in any publications.