SPR with Biotinylated Mouse CDCP1 Protein 5142

Biotinylated Mouse CDCP1 Protein 5142

$525.00 – $1,750.00

Summary

Expression: HEK293
Binding assay: Yes (SPR)
Amino Acid Range: Arg25-Ala667

SKU: 5142parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	C-His-Avi
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Tumor metastasis depends on the dynamic regulation of cell adhesion through β1-integrin. The Cub-Domain Containing Protein-1, CDCP1, is a transmembrane glycoprotein which regulates cell adhesion. Overexpression and loss of CDCP1 have been observed in the same cancer types to promote metastatic progression.
molecular weight	The protein has a predicted MW of 75.3 kDa. Due to glycosylation, the protein migrates to 80-100 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Biotinylated Mouse CDCP1 Protein 5142

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Tumor metastasis depends on the dynamic regulation of cell adhesion through β1-integrin. The Cub-Domain Containing Protein-1, CDCP1, is a transmembrane glycoprotein which regulates cell adhesion. Overexpression and loss of CDCP1 have been observed in the same cancer types to promote metastatic progression.
Protein names CUB domain-containing protein 1 (Membrane glycoprotein gp140) (Transmembrane and associated with src kinases) (CD antigen CD318)
Gene names Cdcp1,Cdcp1
Mass 10090Da
Function May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis.
Subellular location Cell membrane ; Single-pass membrane protein. Note=Its shedding may lead to a soluble peptide.
Structure Interacts with CDH2/N-cadherin, CDH3/P-cadherin, SDC1/syndecan-1, SDC4/syndecan-4 and the serine protease ST14/MT-SP1. Also interacts SRC and PRKCG/protein kinase C gamma (By similarity).
Post-translational modification Phosphorylated on tyrosine by kinases of the SRC family such as SRC and YES as well as by the protein kinase C gamma/PRKCG. Dephosphorylated by phosphotyrosine phosphatases. Also phosphorylated by suramin, a heparin analog. Tyrosine phosphorylated in response to dissociation of integrin alpha-6 beta-4 from laminin-5 (By similarity).; N-glycosylated.; A soluble form may also be produced by proteolytic cleavage at the cell surface (shedding). Another peptide of 80 kDa (p80) is present in cultured keratinocytes probably due to tryptic cleavage at an unidentified site on the N-terminal side. Converted to p80 by plasmin, a trypsin-like protease (By similarity).
Target Relevance information above includes information from UniProt accession: Q5U462
The UniProt Consortium

SPR with Biotinylated Mouse CDCP1 Protein

Anti-CDCP1 Antibody captured on CM5 Chip via Protein A can bind Biotinylated Mouse CDCP-1, His Tag with an affinity constant of 0.45 µM as determined in SPR assay (Biacore T200).

HPLC of Biotinylated Mouse CDCP1 Protein

The purity of Biotinylated Mouse CDCP1 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Biotinylated Mouse CDCP1 Protein

Biotinylated Mouse CDCP1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.