ANTI-COPS5 CLONE 4-9E 25 MIG (C005B-451634)

Specificity

Clone PW-3 is a mouse monoclonal antibody that detects Cell migration-inducing and hyaluronan-binding protein (CEMIP).

Immunogen

V5/His-tagged, full-length, recombinant human Cell migration-inducing and hyaluronan-binding protein (CEMIP).

Application

Quality Control Testing

Evaluated by Western Blotting in DLD-1 cell lysate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected CEMIP in DLD-1 cell lysate.

Tested Applications

Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected CEMIP in Caco-2 and HT29 cell lysates.

Immunohistochemistry Applications: A representative lot detected CEMIP, clone PW-3 in Immunohistochemistry applications (Fink, S.P., et al. (2015). Oncotarget. 6(31):30500-15).

Western Blotting Analysis: A representative lot detected CEMIP in Western Blotting applications (Fink, S.P., et al. (2015). Oncotarget. 6(31):30500-15).

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

Target description

Cell migration-inducing and hyaluronan-binding protein (UniProt: Q8WUJ3; also known as EC:3.2.1.35, CCSP1, CEMIP) is encoded by the CEMIP (also known as KIAA1199) gene (Gene ID: 57214) in human. CEMIP is highly glycosylated protein that is widely distributed in the cytoplasm and is localized in endoplasmic reticulum, endosomes, cell membrane, and in exosomes. It is also abundantly secreted. It is synthesized with a signal peptide (aa 1-30) that is essential for its proper translocation, hyaluronic acid (HA) degradation activity, and secretion. It mediates depolymerization of HA via the cell membrane-associated clathrin-coated pit endocytic pathway. It hydrolyzes high molecular weight HA to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. CEMIP contains two GG domains, one G8 domain (aa 44-166), and four PbH1 domains (aa 572-819). The G8 domain contains eight conserved glycine residues and is reported to bind to Annexin 1 that enables it to adhere to cell membrane in Annexin 1 positive cells. The two GG domains are composed of seven β-strands and two helices and are located N-terminally after the G8 domain. Each of the four PbH1 domains contain 22 to 23 amino acids and function in polysaccharide hydrolysis. Amino acids sequence 295-591, also known as the B domain, is essential for its retention in the endoplasmic reticulum. CEMIP expression is strongly upregulated in many types of cancer and its higher levels are associated with poor prognosis in cancer patients. Higher expression of CEMIP is reported in ductal carcinoma and invasive breast cancer cells, gastric cancers, and in colon adenocarcinomas. It is considered as a potential blood-borne biomarker for colorectal cancers. The knockdown of CEMIP gene has been shown to significantly reduce metastasis to the lung, liver, and various other organs. (Ref.: Domanegg, K., et al (2022). Cancers (Basel). 14(20); 5093; Fink, SP., et al. (2015). Oncotarget, Vol. 6(31); 30500-30515).

Physical form

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Reconstitution

1 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.

Storage and Stability

Recommended storage: +2°C to +8°C.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.