protein

PFDN1 Protein, Mouse (His)

HY-P76541

2 μg;5 μg;10 μg;50 μg

30;55;85;215 USD

PFDN1 Protein, Mouse (His)

proteins

E. coli

2 μg;5 μg;10 μg;50 μg

30;55;85;215 USD

The PFDN1 protein is a key player in the immune response, presenting antigen to CD4 T cells by accommodating 10-30 residue peptides in its peptide-binding cleft. PFDN1 plays a role in the endocytic pathway of antigen-presenting cells, specifically in the exogenous antigen presentation pathway, forming heteromers with three MHC class II molecules and a CD74 trimer in the endoplasmic reticulum. PFDN1 Protein, Mouse (His) is the recombinant mouse-derived PFDN1 protein, expressed by E. coli , with N-His labeled tag. The total length of PFDN1 Protein, Mouse (His) is 122 a.a., with molecular weight of ~16 kDa.

Mouse

HLA-DPB1, a pivotal player in the immune response, is instrumental in presenting peptides derived from antigens to CD4 T-cells. Operating within the endocytic route of antigen-presenting cells (APCs), HLA-DPB1's peptide binding cleft accommodates a range of 10-30 residue peptides. This MHC class II molecule is particularly involved in the exogenous antigen presentation pathway, where peptides from degraded proteins are presented on the cell surface. The complex process involves the association of three MHC class II molecules with a CD74 trimer in the endoplasmic reticulum (ER), forming a heterononamer. Upon entry into the endosomal/lysosomal system, CD74 undergoes sequential degradation, culminating in the release of a small fragment known as CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM, which stabilizes MHC class II molecules until high-affinity antigenic peptides are bound. The resultant MHC II molecule-peptide complex is then transported to the cell membrane surface for recognition. Notably, HLA-DO in B-cells and primary dendritic cells (DCs) regulate the interaction between HLA-DM and MHC class II molecules. The lysosomal microenvironment, characterized by increased acidification, plays a crucial role in regulating antigen loading into MHC II molecules, impacting proteolysis and efficient peptide loading. The heterodimeric structure of HLA-DPB1, composed of an alpha and a beta subunit, contributes to its multifaceted role in antigen presentation.

Prefoldin subunit 1; PFDN1; PFD1

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.