Cat. No. | Product Name | Species | Expression System |
---|---|---|---|
TMPH-00695 |
OmpC Protein, E. coli, Recombinant (His)
Outer membrane protein C... |
E. coli | E. coli |
Forms pores that allow passive diffusion of small molecules across the outer membrane.; (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF.; (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity. | |||
TMPH-00676 |
OmpC Protein, E. coli O157:H7, Recombinant (His & Myc & SUMO)
Outer membrane porin C,Outer<... |
E. coli | E. coli |
Forms pores that allow passive diffusion of small molecules across the outer membrane. | |||
TMPH-00696 |
OmpC Protein, E. coli, Recombinant
Outer membrane protein 1B,Porin O... |
E. coli | E. coli |
Forms pores that allow passive diffusion of small molecules across the outer membrane.; (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF.; (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity. | |||
TMPH-02376 |
OmpC Protein, Klebsiella pneumoniae, Recombinant (His & Myc)
Outer membrane porin C,ompC |
Klebsiella pneumoniae | E. coli |
Forms pores that allow passive diffusion of small molecules across the outer membrane. In K.pneumoniae it has been shown to bind the C1Q component and activate the classical pathway of the complement system. OmpC Protein, Klebsiella pneumoniae, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 45.0 kDa and the accession number is Q48473. | |||
TMPY-02700 |
BCL2 Protein, Human, Recombinant (His)
Bcl-2,PPP1R50,B-cell CLL/lymphoma... |
Human | E. coli |
BCL2 (B-cell leukemia/lymphoma 2, N-Histidine-tagged), also known as Bcl-2, belongs to the Bcl-2 family. Bcl-2 family proteins regulate and contribute to programmed cell death or apoptosis. It is a large protein family and all members contain at least one of four BH (bcl-2 homology) domains. Certain members such as Bcl-2, Bcl-xl and Mcl1 are anti-apoptotic, whilst others are pro-apoptotic. Most Bcl-2 family members contain a C-terminal transmembrane domain that functions to target these proteins... | |||
TMPH-00390 |
MOMP Protein, Chlamydia trachomatis, Recombinant (His & Myc)
ompA,Major outer membrane porin, serovar B |
Chlamydia trachomatis | E. coli |
In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the large cysteine-rich periplasmic protein. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan.; Permits diffusion of specific solutes through the outer membrane. M... | |||
TMPH-00688 |
YbiS Protein, E. coli O6:H1, Recombinant (His & Myc)
Probable L,D-transpeptidase YbiS,ybiS |
E. coli | E. coli |
Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. YbiS Protein, E. coli O6:H1, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 38.3 kDa and the accession number is P0AAX9. | |||
TMPH-00022 |
Outer membrane protein Omp38, Acinetobacter baumannii, Recombinant (His & SUMO)
omp38,Outer membrane protein Omp3... |
Acinetobacter baumannii | E. coli |
Porin. Induces apoptosis in human cells through caspases-dependent and AIF-dependent pathways. Purified Omp38 enters the cells and localizes to the mitochondria, which leads to a release of proapoptotic molecules such as cytochrome c and AIF (apoptosis-inducing factor). Outer membrane protein Omp38, Acinetobacter baumannii, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 52.5 kDa and the accession number is A3M8K2. | |||
TMPH-00318 |
LpxD Protein, Burkholderia pseudomallei, Recombinant (His & Myc)
lpxD,UDP-3-O-acylglucosamine N-ac... |
Burkholderia pseudomallei | E. coli |
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. LpxD Protein, Burkholderia pseudomallei, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 44.2 kDa and the accession number is A3NAT7. | |||
TMPH-03682 |
Varicella-zoster virus (strain Dumas) glycoprotein H/gH Protein (His & Myc)
Envelope glycoprotein H,gH |
HHV-3 | E. coli |
The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis. Varicella-zoster virus (strain Dumas) glycoprotein H/gH Protein (His & Myc) is expressed in E... | |||
TMPH-00023 |
Outer membrane protein Omp38, Acinetobacter baumannii, Recombinant (His & Myc)
Outer membrane protein Omp38,... |
Acinetobacter baumannii | E. coli |
Functions as a porin. Induces apoptosis in human cell lines through caspase-dependent and AIF-dependent pathways. Purified Omp38 enters host cell and localizes to the mitochondria, which presumably leads to a release of proapoptotic molecules such as cytochrome c and AIF (apoptosis-inducing factor). Binds peptidoglycan, contributes to cell wall maintenance (Probable). Outer membrane protein Omp38, Acinetobacter baumannii, Recombinant (His & Myc) is expressed in E. coli expression system with N-1... | |||
TMPK-00418 |
MERTK/Mer Protein, Human, Recombinant (mFc)
MER,Tyro12,MERTK,c-Eyk,MGC133349,c |
Human | HEK293 Cells |
MER tyrosine kinase (MERTK) encodes a surface receptor localized at the apical membrane of the retinal pigment epithelium. It plays a critical role in photoreceptor outer segment internalization prior to phagocytosis. Mutations in MERTK have been associated with severe autosomal recessive retinal dystrophies in the RCS rat and in humans. MERTK/Mer Protein, Human, Recombinant (mFc) is expressed in HEK293 mammalian cells with C-mFc tag. The predicted molecular weight is 78.9 kDa and the accession ... | |||
TMPK-01022 |
MERTK/Mer Protein, Mouse, Recombinant (His)
Tyro12,c-Eyk,MGC133349,RP38,c-mer... |
Mouse | HEK293 Cells |
MER tyrosine kinase (MERTK) encodes a surface receptor localized at the apical membrane of the retinal pigment epithelium. It plays a critical role in photoreceptor outer segment internalization prior to phagocytosis. Mutations in MERTK have been associated with severe autosomal recessive retinal dystrophies in the RCS rat and in humans. MERTK/Mer Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 53.38 kDa and the accession... | |||
TMPK-00417 |
MERTK/Mer Protein, Human, Recombinant (His)
Tyro12,MGC133349,c-mer,MERTK,c-Ey... |
Human | HEK293 Cells |
MER tyrosine kinase (MERTK) encodes a surface receptor localized at the apical membrane of the retinal pigment epithelium. It plays a critical role in photoreceptor outer segment internalization prior to phagocytosis. Mutations in MERTK have been associated with severe autosomal recessive retinal dystrophies in the RCS rat and in humans. MERTK/Mer Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 53.73 kDa and the accession... | |||
TMPH-00759 |
FIV (isolate Petaluma) Gag polyprotein (His & Myc)
Gag polyprotein,gag |
FIV | E. coli |
Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane.; Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.; Nucleocapsid protein p13 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. FIV (isolate Petaluma) Gag polyprotein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted mol... | |||
TMPK-01450 |
HLA-C*03:04&B2M&KRAS G12D (GADGVGKSAL) Monomer Protein, Human, MHC (His & Avi), Biotinylated
KRAS1,MHC,K-RAS4B,KRAS,CFC2,K-RAS... |
Human | HEK293 Cells |
Kirsten rat sarcoma 2 viral oncogene homolog (KRAS) is the most commonly mutated oncogene in human cancer. The developments of many cancers depend on sustained expression and signaling of KRAS, which makes KRAS a high-priority therapeutic target. The virtual screening approach to discover novel KRAS inhibitors and synthetic lethality interactors of KRAS are discussed in detail. | |||
TMPK-01456 |
HLA-C*03:04&B2M&KRAS G12D (GADGVGKSAL) Tetramer Protein, Human, MHC (His & Avi)
KRAS2,NS,MHC,C-K-RAS,KRAS1,K-RAS2A,K-RAS2B... |
Human | HEK293 Cells |
Kirsten rat sarcoma 2 viral oncogene homolog (KRAS) is the most commonly mutated oncogene in human cancer. The developments of many cancers depend on sustained expression and signaling of KRAS, which makes KRAS a high-priority therapeutic target. The virtual screening approach to discover novel KRAS inhibitors and synthetic lethality interactors of KRAS are discussed in detail. | |||
TMPK-01451 |
HLA-C 03:04&B2M&KRAS G12D (GADGVGKSAL) Monomer Protein, Human, MHC (His & Avi)
NS3,K-RAS4A,K-Ras 2,NS,KRAS1,RASK2,MHC,KI-RAS,KRAS,... |
Human | HEK293 Cells |
Kirsten rat sarcoma 2 viral oncogene homolog (KRAS) is the most commonly mutated oncogene in human cancer. The developments of many cancers depend on sustained expression and signaling of KRAS, which makes KRAS a high-priority therapeutic target. The virtual screening approach to discover novel KRAS inhibitors and synthetic lethality interactors of KRAS are discussed in detail. |