Cat. No. | Product Name | Species | Expression System |
---|---|---|---|
TMPY-05220 |
TSLP Protein, Human, Recombinant (R127A & R130S, His)
thymic stromal lymphopoietin |
Human | HEK293 Cells |
TSLP Protein, Human, Recombinant (R127A & R130S, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 16.2 kDa and the accession number is Q969D9-1. | |||
TMPK-00038 |
TSLP Protein, Human, Recombinant (R127A & R130A, His & Avi)
thymic stromal lymphopoietin,TSLP |
Human | HEK293 Cells |
Thymic Stromal Lymphopoietin (TSLP) was originally identified as an activity from the conditioned medium of a mouse thymic stromal cell line that promoted the development of B cells. Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c dendritic cells. Can induce allergic inflammation by directly activating mast cells. TSLP Protein, Human, Recombinant (R127A & R130A, His & Avi) is expressed in HEK293 mammalian cells... | |||
TMPK-00040 |
TSLP Protein, Human, Recombinant (R127A & R130A, His & Avi), Biotinylated
Thymic stromal lymphopoietin,TSLP |
Human | HEK293 Cells |
Thymic Stromal Lymphopoietin (TSLP) was originally identified as an activity from the conditioned medium of a mouse thymic stromal cell line that promoted the development of B cells. Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c dendritic cells. Can induce allergic inflammation by directly activating mast cells. TSLP Protein, Human, Recombinant (R127A & R130A, His & Avi), Biotinylated is expressed in HEK293 m... | |||
TMPK-01523 |
Chimeric HLA-A*02:01 (mα3) &B2M&WT-1 (RMFPNAPYL) Monomer Protein, Human&Mouse, MHC (His & Avi)
WAGR,WT33,AWT1,GUD,RMF,WT1,WIT-2,MHC,NPHS4GUD |
Human & Mouse | HEK293 Cells |
The WT1 protein plays a role in cell growth, the process by which cells mature to perform specific functions (differentiation), and the self-destruction of cells (apoptosis). WT1 is differentially expressed in serous, endometrioid, clear cell, and mucinous carcinomas of the peritoneum, fallopian tube, ovary, and endometrium.The Human HLA-A*0201 WT-1 (RMFPNAPYL) complex Protein is a complex of HLA-A*0201 of the MHC Class I, B2M and RMFPNAPYL peptide of the WT-1. | |||
TMPK-01534 |
Chimeric HLA-A*02:01 (mα3) &B2M&LMP2 (CLGGLLTMV) Monomer Protein, Human&Mouse, MHC (His & Avi)
RING12,PSMB9,Proteasome chain 7,RMF,LMP-2,LMP2,MHC,Macropain... |
Human & Mouse | HEK293 Cells |
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of ma... | |||
TMPK-01522 |
Chimeric HLA-A*02:01 (mα3) &B2M&WT-1 (RMFPNAPYL) Tetramer Protein, Human&Mouse, MHC (His & Avi)
RMF,WT33,WIT-2,MHC,WAGR,AWT1,GUD,WT1,NPHS4GUD |
Human & Mouse | HEK293 Cells |
The WT1 protein plays a role in cell growth, the process by which cells mature to perform specific functions (differentiation), and the self-destruction of cells (apoptosis). WT1 is differentially expressed in serous, endometrioid, clear cell, and mucinous carcinomas of the peritoneum, fallopian tube, ovary, and endometrium.The Human HLA-A*0201 WT-1 (RMFPNAPYL) complex Protein is a complex of HLA-A*0201 of the MHC Class I, B2M and RMFPNAPYL peptide of the WT-1. | |||
TMPK-01535 |
Chimeric HLA-A*02:01 (mα3) &B2M&LMP2 (CLGGLLTMV) Tetramer Protein, Human&Mouse, MHC (His & Avi)
Macropain chain 7,LMP2,Proteasome chain 7,RING12,PSMB9,MHC,R... |
Human & Mouse | HEK293 Cells |
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of ma... |