AFG3L2
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Official Full Name
AFG3 ATPase family gene 3-like 2 (S. cerevisiae)
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Overview
This gene encodes a protein localized in mitochondria and closely related to paraplegin. The paraplegin gene is responsible for an autosomal recessive form of hereditary spastic paraplegia. This gene is a candidate gene for other hereditary spastic paraplegias or neurodegenerative disorders. -
Synonyms
AFG3L2; AFG3 ATPase family gene 3-like 2 (S. cerevisiae); AFG3 (ATPase family gene 3, yeast) like 2 , AFG3 ATPase family gene 3 like 2 (yeast) , SCA28, spinocerebellar ataxia 28; AFG3-like protein 2; AFG3 (ATPase family gene 3, yeast) like 2; AFG3 ATPase family gene 3 like 2 (yeast); AFG3 ATPase family gene 3 like 2; AFG3 like protein 2; ATPase family gene 3 like 2; ATPase family gene 3 yeast; EC 3.4.24.-; FLJ25993; Paraplegin like protein; SCA28; Spinocerebellar ataxia 28; paraplegin-like protein; ATPase family gene 3, yeast;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Homo sapiens (Human)
- Human
- Mouse
- Zebrafish
- E.coli
- E.coli expression system
- HEK293
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- N/A
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Human | AFG3L2-9459H | Recombinant Human AFG3L2, His-tagged | E.coli | His | 449-797a.a. | |
Human | AFG3L2-409H | Recombinant Human AFG3L2 Protein, GST-tagged | Wheat Germ | GST | ||
Human | AFG3L2-26445TH | Recombinant Human AFG3L2, His-tagged | E.coli | His | ||
Human | AFG3L2-8987HCL | Recombinant Human AFG3L2 293 Cell Lysate | HEK293 | N/A | ||
Human | AFG3L2-5205H | Recombinant Human AFG3L2 protein, GST-tagged | E.coli | GST | 550-759aa | |
Human | AFG3L2-990HF | Recombinant Full Length Human AFG3L2 Protein, GST-tagged | In Vitro Cell Free System | GST | 797 amino acids | |
Mouse | AFG3L2-1401M | Recombinant Mouse AFG3L2 Protein | Mammalian Cell | His | ||
Mouse | AFG3L2-376M | Recombinant Mouse AFG3L2 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi | ||
Mouse | AFG3L2-376M-B | Recombinant Mouse AFG3L2 Protein Pre-coupled Magnetic Beads | HEK293 | |||
Homo sapiens (Human) | RFL4960HF | Recombinant Full Length Human Afg3-Like Protein 2(Afg3L2) Protein, His-Tagged | E.coli expression system | His | Full Length (1-797) | |
Zebrafish | AFG3L2-6249Z | Recombinant Zebrafish AFG3L2 | Mammalian Cell | His |
- Involved Pathway
- Protein Function
- Interacting Protein
AFG3L2 involved in several pathways and played different roles in them. We selected most pathways AFG3L2 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with AFG3L2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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AFG3L2 has several biochemical functions, for example, ATP binding, ATP-dependent peptidase activity, metalloendopeptidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by AFG3L2 itself. We selected most functions AFG3L2 had, and list some proteins which have the same functions with AFG3L2. You can find most of the proteins on our site.
Function | Related Protein |
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ATP binding | SCYL1;SRPK1B;KIF2A;TPX2;ADCY9;RFC5;ORC4;CHST13;CDK6 |
ATP-dependent peptidase activity | CRBN;YME1L1;LONP1;LONRF3;SPG7;AFG3L2;LONRF1L;LONRF2 |
metalloendopeptidase activity | ADAM20;THOP1;MMP1;PAPLN;BMP1;ECE2;ASTL;PMPCB;BMP1B |
metallopeptidase activity | ANPEPA;STAMBPA;ADAMTS5;GM12824;ADAM10;BRCC3;ADAM30;ADAMTS4;ADAM8A |
protein binding | CSE1L;BRCA1;HBQ1;INHBB;VPS45;ASCL3;UHRF1;NCOA5;IL1R2 |
unfolded protein binding | PFDN2;CALRL2;NDUFAF1;HSPA8;HSP90B1;CRYABB;DNAJB1A;TOMM20;DNAJB5 |
zinc ion binding | S100A5;CECR1;PDZRN4;ZDHHC20A;BRAP;RBM10;BSPRY;RNF215;FBLIM1 |
AFG3L2 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 AFG3L2 here. Most of them are supplied by our site. Hope this information will be useful for your research of AFG3L2.
BECN1; TNFRSF1A; CLN3; USP50; RAC2; MAPK8IP2; purL; PHC2; RNF167; 15-deoxy-delta(12,14; Trip11; Cenpe; ELL2; E2F3; 1C; Junb; Rc3h2; USF1; Bmpr1a
- Q&As
- Reviews
Q&As (10)
Ask a questionAFG3L2 protein contributes to mitochondrial dynamics, proteostasis, or mitochondrial DNA maintenance, and the underlying molecular mechanisms are currently being investigated.
The subcellular localization of AFG3L2 protein can be experimentally determined using techniques such as immunofluorescence microscopy or subcellular fractionation.
Genetic variations or mutations in the gene encoding AFG3L2 protein may impact its expression or function, influencing mitochondrial dysfunction or neurodegenerative diseases.
Various experimental techniques or assays, such as electron microscopy, protein degradation assays, or animal models, have been used to study the functional significance of AFG3L2 protein.
Dysregulation or dysfunction of AFG3L2 protein can disrupt mitochondrial homeostasis, impair cellular energetics, and contribute to neurodegenerative disease progression.
AFG3L2 protein may interact with specific molecules or participate in protein complexes, which have functional implications in cellular processes.
AFG3L2 protein plays a role in mitochondrial function, protein quality control, or neurodegenerative diseases, and its function can be investigated using techniques like electron microscopy, protein degradation assays, or animal models.
AFG3L2 protein holds potential as a target for modulating mitochondrial function or treating neurodegenerative disorders, and further research is needed to explore its implications for therapeutic interventions.
The expression of AFG3L2 protein is regulated by specific factors and signaling pathways.
Post-translational modifications and regulatory mechanisms may modulate the activity or stability of AFG3L2 protein.
Customer Reviews (3)
Write a reviewDeciphering protein-protein interactions in stem cell differentiation for cellular fate determination.
Exploring protein-protein interactions in RNA metabolism for gene expression regulation.
Elucidating protein-protein interactions in neuronal plasticity for learning and memory.
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