Product nameAnti-TMP21 antibody
See all TMP21 primary antibodies
DescriptionRabbit polyclonal to TMP21
Tested applicationsSuitable for: WBmore details
Unsuitable for: IP
Species reactivityReacts with: Mouse, Human
Predicted to work with: Orangutan
Synthetic peptide within Human TMP21 aa 50-100. The exact sequence is proprietary.
Database link: P49755
- WB: HeLa, HEK-293T, Jurkat, TCMK-1 and NIH/3T3 whole cell lysates.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferPreservative: 0.09% Sodium azide
Constituent: Tris citrate/phosphate
Concentration information loading...
PurityImmunogen affinity purified
Purification notesab241312 was affinity purified using an epitope specific to TMP21 immobilized on solid support.
Our Abpromise guarantee covers the use of ab241312 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/2000 - 1/10000. Predicted molecular weight: 24 kDa.
FunctionInvolved 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.
Sequence similaritiesBelongs to the EMP24/GP25L family.
Contains 1 GOLD domain.
DomainThe lumenal domain mediates localization to the plasma membrane by partially overriding the ER retention by the cytoplasmic domain.
Cellular localizationGolgi 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
- 1110014C03Rik antibody
- 21 kDa transmembrane trafficking protein antibody
- 21 kDa transmembrane-trafficking protein antibody
All lanes : Anti-TMP21 antibody (ab241312) at 0.1 µg/ml
Lane 1 : HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate
Lane 2 : HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate
Lane 3 : Jurkat (human T cell leukemia cell line from peripheral blood) whole cell lysate
Lane 4 : TCMK-1 (Mouse kidney epithelial cell line) whole cell lysate
Lane 5 : NIH/3T3 (Mouse embryo fibroblast cell line) whole cell lysate
Lysates/proteins at 15 µg per lane.
Developed using the ECL technique.
Predicted band size: 24 kDa
Exposure time: 30 seconds
Lysates prepared using NETN lysis buffer.
ab241312 has not yet been referenced specifically in any publications.