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