Rabbit anti-Human ADAM-12 (A Disintigrin And Metalloproteinase-12, Meltrin-alpha) Polyclonal Antibody | anti-ADAM-12 antibody

Anti-ADAM-12 (A Disintigrin And Metalloproteinase-12, Meltrin-alpha), Amino End of Catalytic Domain Antibody

Cat. Num. AAA4157457

• Reactivity: Human
• Applications: Western Blot
• Purity: Immunogen Affinity Purified
• Synonyms: ADAM-12 (A Disintigrin And Metalloproteinase-12; Meltrin-alpha); Polyclonal Antibody; Anti-ADAM-12 (A Disintigrin And Metalloproteinase-12; Amino End of Catalytic Domain Antibody; anti-ADAM-12 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Immunogen Affinity Purified
• Form/Format: Liquid; PBS, pH 7.4 with 0.05% sodium azide.
• Concentration: 1ug/ul (varies by lot)

• Applicable Applications for anti-ADAM-12 antibody: Western Blot (WB)
• Application Notes: WB: 1:1000. The antibody recognizes bands of 116 kDa (minor band), 92 kDa (major band), and cleaved products_recover at 68 kDa, 40 kDa in reduced Western blots of cell lysates. Dilution optimised using Chromogenic detection.
• Immunogen: Synthetic peptide based on the amino end of the catalytic domain of human ADAM 12.
• Cellular Localization: Type I Membrane Protein (isoform 12L). A secreted form (isoform 12S) is produced by alternative splicing
• Preparation and Storage: This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use.; For extended storage, aliquot contents and freeze at-20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Testing Data

Related Product Information for anti-ADAM-12 antibody

Description: The antibody is a rabbit polyclonal antibody made to the metalloproteinase ADAM-12. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human ADAM-12. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant. ADAM-12, also known as Meltrin-?, was first described as a protein participating in myoblast fusion, similar to sperm-egg fusion aided by ADAMs 1 and 2. Later works describe two forms of ADAM-12: ADAM-12-S and ADAM-12-L (short and long forms). The short form is a soluble, alternatively spliced form lacking the transmembrane and Cytoplasmic domains. The short form of ADAM-12 was reported to provoke myogenesis, and the lack of Cytoplasmic domain suggests different regulation pathways (although both forms can be expressed in the same tissue). Other papers investigated SH3 ligand domains in the Cytoplasmic portion of ADAM-12, demonstrating regulation routes for ADAM-12 via Src and Src tyrosine kinase. ADAM-12 is thought to have more limited expression than the other ADAMs originally described in myoblasts (ADAM-9, ADAM-19), and is found mostly in muscle and bone (although placenta, osteoblasts and many tumor cell lines express ADAM-12). ADAM-12 may also act as a cell-attachment molecule, by binding integrins through the cysteine-rich domain. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs), the functions of ADAM-12 are still poorly understood. ADAM-12 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active. Other ADAMs family members (ADAM-10, ADAM-17) have been more thoroughly studied, and are known to play key roles in inflammation, growth factor maturation and release, and a wide range of other functions. The full length ADAM-12 sequence codes for a 909 amino acid protein. Predicted mass is 99.5 kDa, but glycosylation and cyteine-rich regions make the reduced protein run at 114 kDa unprocessed, and 84 kDa processed forms. The soluble ADAM-12 is a 738 AA sequence, predicted at 80.5 kDa, and is seen as a 92 kDa zymogen, and 68 kDa furin processed form. RP3-ADAM-12 recognizes bands of 116 kDa (minor band), 92 kDa (major band), and cleaved products_recover at 68 kDa, 40 kDa in reduced Western blots of cell lysates. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species.

Relevance: ADAM12 is a member of the ADAM (a disintegrin and metalloprotease like domain) family. Two forms of ADAM12 have been described: ADAM12S and ADAM12L (short and long forms). The short form is a soluble form lacking the transmembrane and cytoplasmic domains. The short form of ADAM12 was reported to provoke myogenesis, and the lack of cytoplasmic domain suggests different regulation pathways (although both forms can be expressed in the same tissue). Other papers investigated the SH3 ligand domains in the cytoplasmic portion of ADAM12, demonstrating regulation routes for ADAM12 via Src and Src tyrosine kinase. ADAM12 is primarily expressed in muscle and bone (although placenta, osteoblasts, and many tumor cell lines also express ADAM12). ADAM12 supports cell adhesion by acting as a cell attachment molecule and binding integrins through the cysteine rich domain. A marker of skeletal muscle regeneration, it has been implicated in myoblast differentiation and fusion. ADAM12 contains the canonical HExxHxxxxxH zinc metalloproteinase motif. Full length ADAM12 (909 amino acids) has a predicted mass of 99.5 kDa, but due to glycosylation and cyteine rich regions, the reduced protein migrates to 114 kDa (unprocessed) and 84 kDa (processed). The soluble form of ADAM12 (738 amino acids, predicted mass of 80.5 kDa) is seen as a 92 kDa zymogen and 68 kDa furin processed form