Description: Glycoprotein A33 (GPA33) is also known as Cell surface A33 antigen, is a single-pass type I membrane protein which is expressed in normal gastrointestinal epithelium and in 95% of colon cancers. GPA33 The predicted mature protein has a 213-amino acid extracellular region, a single transmembrane domain, and a 62-amino acid intracellular tail. The sequence of the extracellular region contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain characteristic of the CD2 subgroup of the immunoglobulin (Ig) superfamily, which contains. GPA33 may play a role in cell-cell recognition and signaling.
Description: Glycoprotein A33 (GPA33) is also known as Cell surface A33 antigen, is a single-pass type I membrane protein which is expressed in normal gastrointestinal epithelium and in 95% of colon cancers. GPA33 The predicted mature protein has a 213-amino acid extracellular region, a single transmembrane domain, and a 62-amino acid intracellular tail. The sequence of the extracellular region contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain characteristic of the CD2 subgroup of the immunoglobulin (Ig) superfamily, which contains. GPA33 may play a role in cell-cell recognition and signaling.
Description: Cyclin-Dependent Kinase Inhibitor 1 (CDKN1A) is a member of the CDI family. CDKN1A is widely expressed in all adult tissues, but low expressed in the brain tissue. CDKN1A can be induced by p53/TP53, mezerein and IFNB1, repressed by HDAC1. CDKN1A may be an important intermediate, by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage, CDKN1A can bind to and inhibit cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression.
Description: Protein CutA (CUTA) posseses a signal peptide and is widely expressed in brain. CUTA mayforms part of a complex of membrane proteins attached to acetylcholinesterase (AChE). CUTA takes part in cellular tolerance to a broad range of divalent cations other than copper. Alternate transcriptional splice variants, both protein-coding and non-protein-coding, have been found.
Description: FAM3C, also called interleukin-like EMT inducer, usually exist in most secretory epithelia. It belongs to the FAM3 family according to their sequence similarities. The up-regulation and/or mislocalization in breast cancer and liver carcinoma cells of FAM3C is strongly correlated with metastasis formation and survival. FAM3C can be involved in retinal laminar formation and promote epithelial to mesenchymal transition.
Description: Protein FAM3D is a novel cytokine-like protein that belongs to the FAM3 family. Human FAM3D is synthesized as a 224 amino acid precursor that contains a 25 amino acid signal sequence and a 199 amino acid mature chain. FAM3D is identified based on structural, but not sequence, homology to short chain cytokines including IL-2, IL-4 and GM-CSF. FAM3 proteins are four helix bundle cytokines with four conserved cysteines in all members (FAM3A-D). FAM3B is highly expressed in alpha and beta cells of the pancreas and is being investigated as a potential contributor to beta cell death and development of Type I Diabetes.
Description: Protein G is an immunoglobulin-binding protein expressed in group C and G Streptococcal bacteria much like Protein A but with differing specificities. It is a 65-kDa (G148 protein G) and a 58 kDa (C40 protein G) cell surface protein that has found application in purifying antibodies through its binding to the Fc region. The native molecule also binds albumin, however, because serum albumin is a major contaminant of antibody sources, the albumin binding site has been removed from this recombinant form of Protein G.
Description: Protein L was isolated from the surface of bacterial species Peptostreptococcus magnus and was found to bind Ig(IgG,IgM,IgA,IgE and IgD) through L chain interaction, from which the name was suggested. Despite this wide-ranging binding capability with respect to Ig classes, Protein L is not a universal immunoglobilin-binding protein. Binding of Protein L to immunoglobulins is restricted to those containing kappa light chains (i.e., k chain of the VL domain). In humans and mice, kappa (k) light chains predominate. The remaining immunoglobulins have lambda (l) light chains. The recombinant protein contains four immunoglobulin (Ig) binding domains (Bdomains) of the native protein. Besides antibody, protein L is also suitable for binding of a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs).
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