Recombinant Human ADAMTS-L2 His-tag Protein, CF

Recombinant Human ADAMTS-L2 His-tag Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: ADAMTSL2

ADAMTSL2 (a disintegrin and metalloproteinase with thrombospondin motifs like 2), is one protein from a seven-member family of ADAMTS-like secreted proteins that are related to ADAMTS zinc metalloproteases but do not contain a metalloprotease domain. ADAMTSL2 contains a multidomain structure that includes an N-terminal signal sequence, C-terminal thrombospondin repeats, ADAMTS cysteine-rich and spacer modules, a PLAC domain and an N-glycan rich module unique amongst ADAMTSL family members (1). These domains play a substantial role in ADAMTS specificity and ADAMTSLs are also expected to have specific extracellular ligands. ADAMTSL2 is abundantly expressed in liver, lung, and spleen and resides in the extracellular matrix (ECM) (2). It has been shown to interact with many ECM proteins including fibrillin microfibrils (3), members of the lysyl oxidase family such as LOXL2 (4), and latent transforming growth factor beta binding protein 1 (LTBP1) (5). The interaction between ADAMTSL2 and LTBP1 and fibrillin indicates ADAMTSL2 may have a role in modulation of microfibrillar formation and function (3,5) and ADAMTSL2 has been found upregulated in cardiac fibrosis (6). Through its interaction with the LTBP1 protein and lysyl oxidase family members, ADAMTSL2 protein has been suggested to regulate the availability of TGF-beta and consequent TGF-beta signaling (1,5). Several mutations of ADAMTSL2 lead to a heterogeneous autosomal recessive disease, Geleophysic dysplasia 1 (7, 8). Geleophysic dysplasia 1 may be specifically caused by impaired secretion of ADAMTSL2 due to glycosylation differences (9). A variant of ADAMTSL2 has also been shown to result in an autosomal dominant inherited connective tissue disorder consistent with Ehlers-Danlos syndrome (10).

Related Research Areas

• Metalloproteases and Regulators