AGBL3
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Official Full Name
ATP/GTP binding protein-like 3
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Synonyms
AGBL3; ATP/GTP binding protein-like 3; cytosolic carboxypeptidase 3; MGC32955; ATP/GTP-binding protein-like 3; FLJ12983;
| Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| Human | AGBL3-9466H | Recombinant Human AGBL3, His-tagged | E.coli | His | 272-621a.a. | |
| Mouse | AGBL3-1411M | Recombinant Mouse AGBL3 Protein | Mammalian Cell | His |
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| Mouse | AGBL3-383M | Recombinant Mouse AGBL3 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi |
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| Mouse | AGBL3-383M-B | Recombinant Mouse AGBL3 Protein Pre-coupled Magnetic Beads | HEK293 |
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- Involved Pathway
- Protein Function
- Interacting Protein
AGBL3 involved in several pathways and played different roles in them. We selected most pathways AGBL3 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with AGBL3 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
AGBL3 has several biochemical functions, for example, metallocarboxypeptidase activity, zinc ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AGBL3 itself. We selected most functions AGBL3 had, and list some proteins which have the same functions with AGBL3. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| metallocarboxypeptidase activity | CPA3;FOLH1;CPB1;AGBL4;PEPD;CPD;AGTPBP1;CPDB;CPA6 |
| zinc ion binding | DNAJC21;C6AST4;PDZRN4;MAN2B1;RNF40;DTNA;RSPRY1;DRL;MORC3B |
AGBL3 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AGBL3 here. Most of them are supplied by our site. Hope this information will be useful for your research of AGBL3.
- Q&As
- Reviews
Q&As (20)
Ask a questionAGBL3's interactions with diverse proteins contribute to its cellular roles.
Indeed, AGBL3 expression and activity can be influenced by cellular cues.
Animal models aid in comprehending AGBL3's roles and implications.
AGBL3's potential ties to autophagy, cellular self-degradation, are under investigation.
Yes, AGBL3 displays metalloprotease activity, enabling cleavage of protein peptide bonds.
Yes, AGBL3's presence spans various cell types, indicating widespread involvement.
AGBL3's structure comprises distinctive domains shedding light on its functional roles.
AGBL3's actions are likely integral to maintaining cellular equilibrium.
AGBL3's response to stress is a captivating area under exploration.
Evidence suggests AGBL3 mutations might correlate with specific diseases.
Researchers are investigating AGBL3's viability for therapeutic interventions.
While linked to protein processes, AGBL3's full regulatory roles continue to emerge.
AGBL3's structural domains provide insights into its potential functions.
AGBL3's distinct attributes and roles set it apart from other ATP/GTP-binding proteins.
Animal models aid in comprehending AGBL3's roles and implications.
Ongoing research aims to uncover AGBL3's contributions to cellular signaling networks.
AGBL3's contributions to cellular development are actively explored, suggesting relevance.
AGBL3 represents "ATP/GTP-binding protein-like 3," known for its diverse cellular involvements.
AGBL3 is implicated in various cellular processes, including potential protein regulation.
AGBL3's functions may contribute to maintaining proper protein quality within cells.
Customer Reviews (5)
Write a reviewConsistently achieving specific outcomes validated the crucial role of the product in our studies.
It facilitated efficient protein-protein interaction detection via FRET.
It’s consistent outcomes supported reliable statistical analysis.
Protein's purity was evident in reliable protein crystallization outcomes
The product’s distinct features advanced our research into uncharted territories.
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