Recombinant Human HepaCAM Fc Chimera Protein, CF New

Recombinant Human HepaCAM Fc Chimera 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: HepaCAM

Hepatocyte cell adhesion molecule (HepaCAM), also known as glial cell adhesion molecule (GlialCAM), is a type I transmembrane glycoprotein in the Ig-superfamily that participates in cell migration and proliferation (ref). HepaCAM consists of an extracellular domain (ECD) with two C2 Ig-like domains, a transmembrane region, and an intracellular region containing a SH3 domain. Mature, human HepaCAM shares 99% amino acid sequence identity with mouse HepaCAM.  A second, truncated isoform is known to exist as a result of alternative splicing. Though first detected in the liver, HepaCAM expression has subsequently been detected in glial cells of the central nervous system. HepaCAM forms homodimers, through cis-interactions, on the cell surface and this interaction is known to modulate cell-matrix interactions. HepaCAM has been shown to suppress the growth of hepatocytes and is down-regulated in hepatocellular carcinoma in the liver. In the brain, HepaCAM is normally expressed in astrocytes where it regulates ion homeostasis, BBB physiology, and synaptic excitation. Loss of HepaCAM signaling has been reported to impair gap-junction cell coupling and the balance between synaptic excitation and inhibition. Multiple studies indicate that HepaCAM is a tumor suppressor candidate, but its exact role remains unknown. In Glioblastoma, HepaCAM helps mediate interactions, through its IgG-like domains, with proteins such as Mlc1 and aquaporin-4 and loss of HepaCAM expression results in a proinvasive environment. In prostate cancer, HepaCAM may help inhibit cancer progression as a reduction or absence of HepaCAM expression is seen in majority of cases. Additionally, HepaCAM is suppressed in multiple other carcinomas including breast, kidney, colon, rectum and stomach making it a potential therapeutic target.

Related Research Areas

• Adhesion Molecules in Angiogenesis
• Immunoglobulin Superfamily CAMs