Recombinant Mouse HABP1/C1QBP Protein, CF Summary
Details of Functionality |
Measured by its ability to bind human C1q in a functional ELISA. |
Source |
E. coli-derived mouse HABP1/C1QBP protein Met-Met |
Mouse HABP1 (Leu72-Gln279) Accession # NP_031599 | 6-His tag
| N-terminus | | C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Met |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
C1qbp |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
24.8 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. |
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 MOPS and NaCl with Trehalose. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse HABP1/C1QBP Protein, CF
Background
Hyaluronan binding protein 1 (HABP1), also known as C1qBP/C1qR and p32, is a ubiquitous acidic glycoprotein that functions in spermatogenesis and as a receptor for proinflammatory molecules (1, 2). HABP1 is synthesized with a 71 amino acid (aa) N-terminal preproprotein and a 208 aa mature region (3). The 32 kDa mature mouse HABP1, which contains a MAM33-like sequence, shares 90% and 99% aa sequence identity with human and rat HABP1, respectively. HABP1 assembles into a doughnut shaped trimer, with negatively charged residues asymmetrically distributed on one face lining the channel of the complex (4). HABP1 can be cleaved by cell surface MMP-14/MT1-MMP, a protease important in angiogenesis and tumor metastasis (5). Cell surface HABP1 binds a wide range of extracellular molecules, including hyaluronan, vitronectin, complement component C1q, HMW kininogen, and bacterial and viral proteins (2, 6 - 9). Within the cell, HABP1 binds to molecules containing the C1q globular domain, multiple isoforms of PKC, mitochondrial Hrk, the cytoplasmic tails of adrenergic and GABA-A receptors, the mRNA splicing factor ASF/SF2, and the CBF transcription factor (10 - 16). Apoptosis and direct phosphorylation by Erk1/2 induces HABP1 translocation to the nucleus (17).
- Thakur, S.C. et al. (2006) J. Androl. 27:604.
- Peerschke, E.I.B. and B. Ghebrehiwet (2007) Immunobiology 212:333.
- Lynch, N.J. et al. (1997) FEBS Lett. 418:111.
- Jiang, J. et al. (1999) Proc. Natl. Acad. Sci. 96:3572.
- Rozanov, D.V. et al. (2002) J. Biol. Chem. 277:9318.
- Deb, T.B. and K. Datta (1996) J. Biol. Chem. 271:2206.
- Lim, B.L. et al. (1996) J. Biol. Chem. 271:26739.
- Grebrehiwet, B. et al. (1994) J. Exp. Med. 179:1809.
- Waggoner, S.N. et al. (2007) J. Leukoc. Biol. 82 epub. 291:829.
- Innamorati, G. et al. (2006) Cell. Signal. 18:761.
- Robles-Flores, M. et al. (2002) J. Biol. Chem. 277:5247.
- Sunayama, J. et al. (1994) Cell Death Differ. 11:771.
- Pupo, A.S. and K.P. Minneman (2003) J. Recept. Signal Transduct. Res. 23:185.
- Schaerer, M.T. et al. (2001) J. Biol. Chem. 276:26597.
- Peterson-Mahrt, S.K. et al. (1999) EMBO J. 18:1014.
- Chattopadhyay, C. et al. (2004) Nucleic Acids Res. 32:3632.
- Majumdar, M. et al. (2002) Biochem. Biophys. Res. Commun. 291:829.
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