Rabbit Antibody to ADAM-33   (A Disintegrin And Metalloproteinase-33); Propeptide domain

RP1-ADAM-33 is a polyclonal antibody made to the metalloproteinase ADAM-33.   The antibody is made to a synthetic peptide based on the amino end of human ADAM-33.   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-33 was first described from mouse brain, as an ADAM protease containing the conserved disintegrin domains found in other family members.   Both human and mouse ADAM-33 were cloned, and have relatively high identity (71%), but lower identity (37%) with xenopus ADAM-13 (thought to be a species orthologue).   ADAM-33 maps to chromosome 20 in humans and to chromosome 2 in mouse.   A second sequence, alternatively spliced, has been reported for both human and mouse ADAM-33.   The smaller sequence lacks exon #17, leading to a shorter EGF-like domain.   ADAM-33 appears to be widely expressed, found in most organs analyzed.   Testis showed a smaller message than other tissues, and may represent a truncated form of ADAM-33.   ADAM-33 does not contain SH3 ligand domains in the Cytoplasmic portion, as ADAM-13 does, and thus may be differently regulated.   ADAM-33 may also act as a cell-attachment molecule, by binding integrins through the cysteine-rich domain.   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.   Recent work suggests that mutations in ADAM-33 may be linked to asthma; indeed, many of the mutations generate new cysteine residues, which may well disturb ADAM-33 function.   ADAM-33 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine-rich, EGF-like, transmembrane and Cytoplasmic domains.   The full length human ADAM-33 sequence codes for a 813 amino acid protein, with predicted mass of 87.739kD, but glycosylation and cyteine-rich regions give ADAM-33 an apparent MW of 99 kD on reduced SDS-PAGE gels.   The smaller sequence is 728 amino acids, predicting a 78.319 kD zymogen.   Mouse sequences are 797 and 685 amino acids, predicting 87.009 and 74.719 kD proteins, respectively, before post-translational modifications.   ADAM-33 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain.   RP1-ADAM-33 recognizes bands of 99 kD (minor band), 58 kD (major band), and cleaved products 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.

FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS.

The undiluted antibody solution is stable for approximately 6 months at   4 °C. For longer storage, store at   -20 °C .

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