Recombinant Human HepaCAM Fc Chimera Protein, CF

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2 μg/lane of Recombinant Human HepaCAM Fc Chimera Protein (Catalog # 11598-HC) was resolved with SDS-PAGE under reducing (R) condition and visualized by Coomassie® Blue staining, showing bands at 60-80 kDa, under ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human HepaCAM Fc Chimera Protein, CF Summary

Details of Functionality
Bioassay data are not available.
Source
Chinese Hamster Ovary cell line, CHO-derived human HepaCAM protein
Human HepaCAM
(Val34-Ser240)
Accession # Q19CZ8.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
N-terminal Sequence
Val34
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
50 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
60-80 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human HepaCAM Fc Chimera Protein, CF

  • cancer susceptibility
  • FLJ25530
  • glial cell adhesion molecule
  • GlialCAM
  • HepaCAM
  • hepatic and glial cell adhesion molecule
  • hepatocyte cell adhesion molecule
  • Protein hepaCAM

Background

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.
  1. Moh, M. C., et al. (2005) J. Hepatol. 42:833.
  2. Moh, M.C., et al. (2005) 280:27366.
  3. Sofroniew, M.V. (2021) Neuron 109:2365.
  4. Baldwin, K.T. et al. (2021) Neuron 109:2427.
  5. De, A., et al. (2023) J Neurosci. 43:8043.
  6. Deng Q, et al. (2019) Mol Med Rep 19:2115.
  7. Moh, M.C., et al. (2008) Carcinogenesis 29:2298.

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