p-2

Myelin P2 protein, also known as PMP2, is a cytosolic protein found primarily in peripheral nerves. It Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. It is similar in amino acid sequence and tertiary structure to fatty acid binding proteins found in the liver, adipocytes, and intestine, its expression is limited to the nervous system. PMP2 is detected only in myelin-producing cells of the central and peripheral nervous systems, the oligodendrocytes and Schwann cells, respectively. PMP2 may play a role in lipid transport protein in Schwann cells. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

Expression system: E. coli
Length: 16-141, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-206, Full Length of Isoform 2
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 24-99, Full Length of Mature Protein
Activity: Not Tested

Hypersensitivity to house dust mite (Dermatophagoides sp.) allergens is one of the most common allergic reactions in the world. The house dust mite allergen, Der p 2, is a major allergen and 80–90% of patients who react to mite extract, react specifically to this protein or its homologues. Although it is well characterized in terms of allergenicity, there is still some ambiguity in terms of its biological function. Three-dimensional structural analysis of Der p 2 and its close homologues indicate the presence of a hydrophobic cavity which can potentially bind to lipid molecules.

Phl p 2 Protein, Phleum pratense, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 13.1 kDa and the accession number is P43214-1.

SARS-CoV-2 (P.1) Spike S1+S2 trimer Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 136.59 kDa and the accession number is YP_009724390.1.

Expression system: E. coli
Length: 283-396, Full Length of Mature Protein
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 108-483, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 108-483, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 42-575, Extracellular Domain
Activity: Not Tested

Expression system: E. coli
Length: 24-203, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 131-153, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 108-539, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-206, Full Length
Activity: Not Tested

MMP-21 Protein, Mouse, Recombinant is expressed in E. coli. The accession number is Q8K3F2.

Expression system: HEK293 Cells
Length: 27-220, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 27-274, Partial
Activity: BLI、ELISA

Expression system: HEK293 Cells
Length: 88-274, Partial
Activity: ELISA

Expression system: HEK293 Cells
Length: 27-274, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-220, Partial
Activity: Not Tested

72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene.It belongs to the matrix metalloproteinase (MMP) family. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMP-2 is ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, atherosclerotic plaque rupture, as well as degrading extracellular matrix proteins. MMP-2 can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. MMP-2 cleaves KISS at a Gly-|-Leu bond and appears to have a role in myocardial cell death pathways.

Mouse Metalloproteinase inhibitor 2(TIMP-2), belongs to a family of proteins that regulate the activation and proteolytic activity of matrix metalloproteinases (MMPs). There are four mammalian members of the family; TIMP‑1, TIMP‑2, TIMP‑3, and TIMP‑4. The TIMP-2 is detected in testis, retina, hippocampus and cerebral cortex. The function of TIMP 2 protein is to inhibit MMPs non covalently by the formation of binary complexes. Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.And the interaction with MMP-14 facilitates the activation of pro-MMP-2.It has been shown that the binding of TIMP 2 to a3b1 integrin results in the inhibition of endothelial cell proliferation and angiogenesis.

Expression system: E. coli Length: 283-396, Full Length of Mature Protein Activity: Cell Activity