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Mouse Anti-AGK Recombinant Antibody (V2-258056) (CBMAB-M0989-FY)

This product is mouse antibody that recognizes AGK. The antibody CBFYM-0842 can be used for immunoassay techniques such as: WB, IP, IF, ELISA.
See all AGK antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Mouse, Rat, Human
Clone
V2-258056
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 377-398 near the C-terminus of MULK of human origin.
Host Species
Mouse
Specificity
Mouse, Rat, Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate).
IF(ICC)1:50-1:500
ELISA1:100-1:2,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
acylglycerol kinase
Introduction
The protein encoded by this gene is a mitochondrial membrane protein involved in lipid and glycerolipid metabolism. The encoded protein is a lipid kinase that catalyzes the formation of phosphatidic and lysophosphatidic acids. Defects in this gene have been associated with mitochondrial DNA depletion syndrome 10.
Entrez Gene ID
Human55750
Mouse69923
Rat502749
UniProt ID
HumanQ53H12
MouseQ9ESW4
RatD3Z9L0
Alternative Names
Acylglycerol Kinase; Multiple Substrate Lipid Kinase; Multi-Substrate Lipid Kinase; HsMuLK; MULK; HAGK; Acylglycerol Kinase, Mitochondrial
Function
Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Phosphorylates ceramide (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex. The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth.
Biological Process
Ceramide biosynthetic process
Glycerophospholipid biosynthetic process
Phosphorylation
Protein insertion into mitochondrial inner membrane
Sphingolipid metabolic process
Sphingosine biosynthetic process
Cellular Location
Mitochondrion inner membrane; Mitochondrion intermembrane space. Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it.
Involvement in disease
Mitochondrial DNA depletion syndrome 10 (MTDPS10): The TIM22 complex and import of proteins into mitochondrion are affected in patients suffering of MTDPS10. An autosomal recessive mitochondrial disorder characterized by congenital cataracts, hypertrophic cardiomyopathy, skeletal myopathy, exercise intolerance, and lactic acidosis. Mental development is normal, but affected individuals may die early from cardiomyopathy.
Cataract 38 (CTRCT38): An opacification of the crystalline lens of the eye becoming evident at birth. It frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function.

Sun, F., Ma, Y., Jie, Q., & Li, Q. (2021). P–422 Acylglycerol Kinase is a new novel marker in preeclampsia. Human Reproduction, 36(Supplement_1), deab130-421.

Zhao, C., Chen, H. Y., Zhao, F., Feng, H. J., & Su, J. P. (2021). Acylglycerol kinase promotes paclitaxel resistance in nasopharyngeal carcinoma cells by regulating FOXM1 via the JAK2/STAT3 pathway. Cytokine, 155595.

Zhu, Q., Zhong, A. L., Hu, H., Zhao, J. J., Weng, D. S., Tang, Y., ... & Xia, J. C. (2020). Acylglycerol kinase promotes tumour growth and metastasis via activating the PI3K/AKT/GSK3β signalling pathway in renal cell carcinoma. Journal of hematology & oncology, 13(1), 1-16.

Huang, S., Cao, Y., Guo, H., Yao, Y., Li, L., Chen, J., ... & Xiong, J. (2020). Up‐regulated acylglycerol kinase (AGK) expression associates with gastric cancer progression through the formation of a novel YAP1‐AGK–positive loop. Journal of cellular and molecular medicine, 24(19), 11133-11145.

Zhao, Q., Sun, P., Qin, S., & Liu, J. (2020). Acylglycerol kinase promotes the stemness of nasopharyngeal carcinoma cells by promoting β‐catenin translocation to the nucleus through activating PI3K/Akt pathway. Environmental Toxicology, 35(12), 1299-1307.

Hu, Z., Qu, G., Yu, X., Jiang, H., Teng, X. L., Ding, L., ... & Zou, Q. (2019). Acylglycerol kinase maintains metabolic state and immune responses of CD8+ T cells. Cell metabolism, 30(2), 290-302.

Vukotic, M., Nolte, H., König, T., Saita, S., Ananjew, M., Krüger, M., ... & Langer, T. (2017). Acylglycerol kinase mutated in Sengers syndrome is a subunit of the TIM22 protein translocase in mitochondria. Molecular cell, 67(3), 471-483.

Kang, Y., Stroud, D. A., Baker, M. J., De Souza, D. P., Frazier, A. E., Liem, M., ... & Stojanovski, D. (2017). Sengers syndrome-associated mitochondrial acylglycerol kinase is a subunit of the human TIM22 protein import complex. Molecular cell, 67(3), 457-470.

Mårtensson, C. U., & Becker, T. (2017). Acylglycerol kinase: mitochondrial protein transport meets lipid biosynthesis. Trends in cell biology, 27(10), 700-702.

Houten, S. M. (2017). Protein moonlighting in inborn errors of metabolism: The case of the mitochondrial acylglycerol kinase. Journal of inherited metabolic disease, 40(6), 755.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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