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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for SPARC-like 1/SPARCL1 Antibody [Biotin]
Hevin
High endothelial venule protein
MAST 9
MAST9
PIG33
proliferation-inducing protein 33
SC1
SPARC like 1
SPARCL1
SPARC-like 1 (hevin)
SPARC-like 1 (mast9, hevin)
SPARC-like 1
SPARC-like protein 1
Background
SPARCL1 (Secreted Protein, Acidic and Rich in Cysteines‑like 1), also known as hevin, SC1 or MAST9, is a member of the SPARC family of extracellular glycoproteins (1, 2). SPARCL1 is an anti‑adhesive protein that is widely expressed in tissues such as brain, heart, lung, muscle and kidney, but not liver (3, 4). Human SPARCL1 contains a 16 amino acid (aa) signal sequence and a 648 aa mature region with four domains: a 416 aa N‑terminal acidic region, a 23 aa follistatin‑like domain, a 55 aa kazal‑like segment and a 48 aa EF‑hand/calcium‑binding domain (3, 4). SPARCL1 is predicted at 75 kDa, but migrates at ~130 kDa, which has been explained either by disulfide‑linked homodimerization or by glycosylation and high acidity (3‑5). Some truncated forms have been reported. In mouse, a 55 kDa C‑terminal fragment is the only form in kidney and represents a portion of SPARCL1 in other tissues (6). In humans, a 25 kDa form is increased in liver tumors that are encapsulated, while the full‑length form is down‑regulated in many epithelial cell‑derived tumors (7, 8). SPARCL1 inhibits adhesion and spreading on a variety of substrates (5, 9). It is thought to cause antiadhesive signaling that terminates neuronal migration, consistent with production by glial and neuronal cells during development or in response to trauma (10). In tonsillar high endothelial venules (HEV), SPARCL1 may induce endothelial cell dissociation, promoting extravasation (3). SPARCL1 binds collagen; in mice, deletion causes dermal collagen fibrils that are smaller in diameter and deficient in decorin (6, 11). Human mature SPARCL1 shares 67%, 69%, 78%, 76%, 72% and 72% aa identity with mouse, rat, equine, canine, porcine and bovine SPARCL1, respectively. The follistatin‑like, kazal-like and calcium-binding domains of SPARCL1 show 61% aa identity with corresponding regions of SPARC.
Framson, P. E. and E. H. Sage (2004) J. Cell. Biochem. 92:679.
Sullivan, M. M. and E. H. Sage (2004) Int. J. Biochem. Cell Biol. 36:991.
Girard, J. P. and T. A. Springer (1995) Immunity 2:113.
Bendik, I. et al. (1998) Cancer Res. 58:626.
Brekken, R. A. et al. (2004) J. Histochem. Cytochem. 52:735.
Hambrock, H. O. et al. (2003) J. Biol. Chem. 278:11351.
Lau, C. P. et al. (2006) J. Pathol. 210:469.
Isler, S. G. et al. (2001) Int. J. Oncol. 18:521.
Girard, J. P. and T. A. Springer (1996) J. Biol. Chem. 271:4511.
Gongidi, V. et al. (2004) Neuron 41:57.
Sullivan, M. M. et al. (2006) J. Biol. Chem. 281:27621.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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