Recombinant Lymphocytic choriomeningitis virus Pre-glycoprotein polyprotein... Reference: CSB-BP362127LKZ1_500 Glycoprotein G2: class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.Stable signal peptide: cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.Glycoprotein G1: interacts with the host receptor.
Recombinant Lymphocytic choriomeningitis virus Pre-glycoprotein polyprotein... Reference: CSB-BP362127LKZ1_100 Glycoprotein G2: class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.Stable signal peptide: cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.Glycoprotein G1: interacts with the host receptor.
Recombinant Lymphocytic choriomeningitis virus Pre-glycoprotein polyprotein... Reference: CSB-BP362127LKZ1_20 Glycoprotein G2: class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.Stable signal peptide: cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.Glycoprotein G1: interacts with the host receptor.
Recombinant Bovine Odorant-binding protein Reference: CSB-BP362133BO_100 This protein binds a wide variety of chemical odorants.
Recombinant Bovine Odorant-binding protein Reference: CSB-BP362133BO_10 This protein binds a wide variety of chemical odorants.
Recombinant Vaccinia virus Protein L1(VACWR088),partial Reference: CSB-BP362178VAI1_1 Envelope protein which probably plays a role in virus entry into the host cell. Is probably involved in the virus attachment to the host cell surface and associates with the entry/fusion complex (EFC). Needed for fusion and penetration of the virus core into host cell.
Recombinant Vaccinia virus Protein L1(VACWR088),partial Reference: CSB-BP362178VAI1_100 Envelope protein which probably plays a role in virus entry into the host cell. Is probably involved in the virus attachment to the host cell surface and associates with the entry/fusion complex (EFC). Needed for fusion and penetration of the virus core into host cell.
Recombinant Vaccinia virus Protein L1(VACWR088),partial Reference: CSB-BP362178VAI1_20 Envelope protein which probably plays a role in virus entry into the host cell. Is probably involved in the virus attachment to the host cell surface and associates with the entry/fusion complex (EFC). Needed for fusion and penetration of the virus core into host cell.
Recombinant Gallus gallus Heat shock 70 kDa protein,partial Reference: CSB-BP362326CH_1 Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.
Recombinant Gallus gallus Heat shock 70 kDa protein,partial Reference: CSB-BP362326CH_100 Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.
Recombinant Gallus gallus Heat shock 70 kDa protein,partial Reference: CSB-BP362326CH_20 Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.