Human CUB Domain Containing Protein 1 (CDCP1) Protein
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935106861
info@markelab.com
Precio
312€ (1 µg)
Protein CDCP1
proveedor
Abbexareference
abx680187Tested Applications
SDS-PAGEreactivity
status
RUOclonality
Descripción
Human CUB Domain Containing Protein 1 (CDCP1) Protein is a recombinant protein produced in Sf9, Baculovirus cells.
Background
CDCP1 (CUB Domain Containing Protein 1), also known as CD318 or Trask, is a transmembrane protein widely expressed across cell types, including epithelial cells, stem cells, and notably in certain types of cancer cells. CDCP1 is known for its involvement in various cellular processes, including cell adhesion, migration, and signal transduction. It is a single-pass membrane protein characterized by extracellular CUB domains, which are implicated in protein-protein interactions, especially in cell communication and adhesion mechanisms. CDCP1 plays a crucial role in cancer biology, as its overexpression or aberrant activation has been observed in multiple malignancies, such as lung, colon, and breast cancer, where it contributes to processes like invasion, metastasis, and resistance to apoptosis. This makes CDCP1 an important molecule in cancer progression and a potential target for therapeutic interventions. Moreover, CDCP1 is implicated in non-cancerous biological pathways, including wound healing and tissue remodeling, which involve dynamic changes in cell adhesion and migration.
Características del producto
category
Proteins and Peptides
origin
Human
host
Insect
immunogen target
CUB Domain Containing Protein 1 (CDCP1)
host
Insect
conjugation
Unconjugated
form
Liquid
tested applications
SDS-PAGE
size 1
1 µg
size 2
5 µg
size 3
25 µg
expression
Recombinant
purity
> 90% (SDS-PAGE)
or code
CDCP1
dry ice
No
availability
Shipped within 5-10 working days.
alias
Membrane glycoprotein gp140,CD318,TRASK,SIMA135,Subtractive immunization M plus HEp3-associated 135 kDa protein
note
This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use.
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