Native Proteins and Derivatives
Cayman Chemical G9alike protein human recomb
Active recombinant N-terminal GST-tagged protein expressed in E. coli • G9a-like protein (GLP) is a SET domain-containing methyltransferases that specifically mono- and di-methylate histone H3 at lysine 9 (H3K9).
Biotium MAP3K1 Mitogen-Activated Protein Kinase Kinase Kinase 12F6 CF647 conjugate 0.1mgmL
MAP3K1 Mitogen-Activated Protein Kinase Kinase Kinase 12F6 CF647 conjugate 0.1mgmL
Medchemexpress LLC C1q Protein (Mouse) | ≥92% | 100 UG
C1q Protein (mouse) is a complement protein and a recognition molecule of the classical pathway, performing diverse complement and non-complement functions. It binds various ligands derived from self, non-self, and altered self, modulating the functions of immune and non-immune cells, and can be used for the research of multiple diseases.
- Activates canonical Wnt signaling
- Modulates immune cell differentiation and activation
- Induces apoptosis
- Augments phagocytosis
- Tags synapses for elimination
- Promotes angiogenesis
- Facilitates pathogen clearance
- Modulates prion uptake
- Exhibits neuroprotection
- Supports placentation
- Restores normal angiogenesis in skin wounds of C1q-deficient mice
Waters Corp Native PFAS Precision and Recovery Standard Solution
Native PFAS Precision and Recovery Standard Solution
ILEX LIFE SCIENCES LLC BATROXOBIN PROTEIN 50 UG
Ilex Life Sciences Batroxobin, Native Protein (50 ug). DESCRIPTION: Batroxobin, Native Protein, isolated from Bothrops atrox snake venom, has a molecular weight of approximately 43 kDa. Batroxobin is a serine protease that reduces fibrinogen levels via selective cleavage of Arg-Gly bonds in fibrinogen alpha chains (FGA) to form fibrin and release fibrinopeptide A. Batroxobin is closely related in physiological function and molecular size to thrombin. Unlike thrombin, Batroxobin is not affected by heparin and hirudin. FORMULATION: Sterile filtered white lyophilized (freeze-dried) powder. The Batroxobin protein was lyophilized from a concentrated (1 mg/ml) solution with no additives. BIOACTIVITY: 100 BU (Batroxobin Units) per milligram. SYNONYMS: Thrombin-like enzyme batroxobin, EC:3.4.21.74, BX, SVTLE, Bothrops atrox serine proteinase, Fibrinogen-clotting enzyme, Reptilase, Snake venom serine protease (SVSP), Venombin A, UniProtKB# P04971.
ILEX LIFE SCIENCES LLC BATROXOBIN PROTEIN 10 UG
Ilex Life Sciences Batroxobin, Native Protein (10 ug). DESCRIPTION: Batroxobin, Native Protein, isolated from Bothrops atrox snake venom, has a molecular weight of approximately 43 kDa. Batroxobin is a serine protease that reduces fibrinogen levels via selective cleavage of Arg-Gly bonds in fibrinogen alpha chains (FGA) to form fibrin and release fibrinopeptide A. Batroxobin is closely related in physiological function and molecular size to thrombin. Unlike thrombin, Batroxobin is not affected by heparin and hirudin. FORMULATION: Sterile filtered white lyophilized (freeze-dried) powder. The Batroxobin protein was lyophilized from a concentrated (1 mg/ml) solution with no additives. BIOACTIVITY: 100 BU (Batroxobin Units) per milligram. SYNONYMS: Thrombin-like enzyme batroxobin, EC:3.4.21.74, BX, SVTLE, Bothrops atrox serine proteinase, Fibrinogen-clotting enzyme, Reptilase, Snake venom serine protease (SVSP), Venombin A, UniProtKB# P04971.
ILEX LIFE SCIENCES LLC PORCINE THROMBIN PROTEIN 2 KU
Ilex Life Sciences Thrombin Porcine, Purified Protein (2000 U). DESCRIPTION: Thrombin Porcine, purified native enzyme, lyophilized. CAS REGISTRY NO.: 9002-04-4. FORMULATION: Sterile filtered white lyophilized (freeze-dried) powder. Lyophilized powder from glycine, calcium chloride pH 7.0 containing 0.9% NaCl. OTHER NAMES: Native thrombin protein, Porcine Activated Factor IIa, Factor 2A, F2, PT, RPRGL2, THPH1, coagulation factor II, EC 3.4.21.5, UniProtKB# P00735. APPLICATION: As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.