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ADAM12 Matched Antibody Pair (024) (APMAB-024LY)

This antibody pair set can be used for detecting and quantifying protein level of human ADAM12.
See all ADAM12 antibodies

Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Mouse anti-ADAM12 monoclonal, IgG1 antibody, 100 ug
Detection Antibody
Anti-ADAM12 Rabbit polyclonal antibody, 50 ug
Dilutions
10 ng/ml-100 ng/ml
Format
Liquid
Storage
Aliquot and store at -20°Cor -80°C. Avoid freeze-thaw cycles.
Introduction
This gene encodes a member of a family of proteins that are structurally related to snake venom disintegrins and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. Expression of this gene has been used as a maternal serum marker for pre-natal development. Alternative splicing results in multiple transcript variants encoding different isoforms. Shorter isoforms are secreted, while longer isoforms are membrane-bound form. [provided by RefSeq, Jan 2014]
Alternative Names
ADAM Metallopeptidase Domain 12; Meltrin-Alpha; MLTN; Disintegrin And Metalloproteinase Domain-Containing Protein 12; A Disintegrin And Metalloproteinase Domain 12 (Meltrin Alpha); Metalloprotease-Disintegrin 12 Transmembrane; Meltrin Alpha; EC 3.4.24.58; EC 3.4.24.-;
Entrez Gene ID
8038
UniProt ID
O43184

Mohamad, A., Hassan, R., Azlan Husin, M. F. J., & Sulong, S. (2021). Aberrant Methylation of Tumour Suppressor Gene ADAM12 in Chronic Lympocytic Leukemia Patients: Application of Methylation Specific-PCR Technique. Asian Pacific Journal of Cancer Prevention: APJCP, 22(1), 85.

Wang, L., Tan, Z., Zhang, Y., Kady Keita, N., Liu, H., & Zhang, Y. (2020). ADAM12 silencing promotes cellular apoptosis by activating autophagy in choriocarcinoma cells. International journal of oncology, 56(5), 1162-1174.

Bernstein, H. G., Keilhoff, G., Dobrowolny, H., Lendeckel, U., & Steiner, J. (2020). From putative brain tumor marker to high cognitive abilities: Emerging roles of a disintegrin and metalloprotease (ADAM) 12 in the brain. Journal of Chemical Neuroanatomy, 101846.

Aguilar Muniz, L. S., Gonzalez Galarza, F. F., Arguello Astorga, R., Prieto Hinojosa, A. I., Hernandez Teran, F., Mendez Hernandez, A., ... & Arellano Pérez Vertti, R. D. (2020). Analyses of the Genetic Polymorphisms rs3740199 and rs1871054 of the ADAM12 Gene and the Alleles at the rs2073508 Loci of the TGFB1 Gene and Their Contribution to Susceptibility to Primary Knee Osteoarthritis. Genetic testing and molecular biomarkers, 24(6), 375-380.

Albrechtsen, R., Wewer Albrechtsen, N. J., Gnosa, S., Schwarz, J., Dyrskjøt, L., & Kveiborg, M. (2019). Identification of ADAM12 as a novel basigin sheddase. International journal of molecular sciences, 20(8), 1957.

Xiong, L., Yan, W., Zubia, E., Zhou, Y., Zhang, Y., Duan, Q., ... & Xu, G. (2018). Quantitative proteomics and biochemical analyses reveal the role of endoplasmin in the regulation of the expression and secretion of A Disintegrin And Metalloproteinase 12. Journal of proteomics, 182, 34-44.

Hu, X., Sun, G., & Wang, W. (2017). Association of ADAM 12 polymorphisms with the risk of knee osteoarthritis: meta-analysis of 5048 cases and 6848 controls. Rheumatology international, 37(10), 1659-1666.

Wu, Z., Xu, X. W., & Zhang, X. W. (2017). The association of ADAM12 polymorphism with osteoarthritis susceptibility: a meta-analysis. Therapeutics and clinical risk management, 13, 821.

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

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