Anti-VPS29 antibody (133-183) (STJ503500)

SPECIFICATIONS
ClonalityPolyclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenSynthetic peptide taken within amino acid region 133-183 on rat Vacuolar Protein Sorting-Associated Protein 29.
STJ503500-100
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General Information

Short DescriptionRabbit polyclonal antibody anti-VPS29 (133-183) is suitable for use in ELISA, Immunohistochemistry, Immunoprecipitation and Western Blot research applications.
ApplicationsELISA/IHC/IP/WB
HostRabbit
ReactivityChicken/Human/Mouse/Rat
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityPolyclonal
IsotypeIgG
ConjugationUnconjugated
Concentration0.50-1.50 µg/µl
PurificationAffinity Purified
Dilution RangeWB: 1:500
DB: 1:10, 000
ELISA: 1:10, 000
IP: 1:200
IHC: 1:50-1:100
FormulationContains Tris, HCl/Glycine buffer pH 7.4-7.8, 30% Glycerol and 0.5% BSA, along with cryo-protective agents, Hepes, and long-term preservatives (0.02% Sodium Azide).
Storage InstructionStore at-20°C for long term storage. Avoid freeze-thaw cycles.

Target Information

Gene SymbolVPS29
Gene ID51699
Uniprot IDVPS29_HUMAN
ImmunogenSynthetic peptide taken within amino acid region 133-183 on rat Vacuolar Protein Sorting-Associated Protein 29.
Immunogen Region133-183

Additional Info

Tissue Specificity Ubiquitous. Highly expressed in heart, lung, placenta, spleen, peripheral blood leukocytes, thymus, colon skeletal muscle, kidney and brain.
Function Acts as a component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Acts also as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). In the endosomes, retriever complex drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. Involved in GLUT1 endosome-to-plasma membrane trafficking.the function is dependent of association with ANKRD27. (Microbial infection) The heterotrimeric retromer cargo-selective complex (CSC) mediates the exit of human papillomavirus from the early endosome and the delivery to the Golgi apparatus.
Protein Name Vacuolar Protein Sorting-Associated Protein 29
Hvps29
Pep11 Homolog
Vesicle Protein Sorting 29
Database Links Reactome: R-HSA-3238698
Cellular Localisation Cytoplasm
Membrane
Peripheral Membrane Protein
Endosome Membrane
Early Endosome
Late Endosome
Alternative Antibody Names Anti-Vacuolar Protein Sorting-Associated Protein 29 antibody
Anti-Hvps29 antibody
Anti-Pep11 Homolog antibody
Anti-Vesicle Protein Sorting 29 antibody
Anti-VPS29 antibody
Anti-DC15 antibody
Anti-DC7 antibody
Anti-MDS007 antibody

Information sourced from Uniprot.org

Citations

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