wound

Expression system: E. coli
Length: 38-208, Full Length of Mature Protein
Activity: Organoid Coculture、Cells

Expression system: HEK293 Cells
Length: 21-417, Partial
Activity: ELISA

Expression system: E. coli
Length: 26-187, Full length of the mature protein
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 26-187, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 44-622, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 1-323, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 105-472, Full Length of Mature Protein
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 28-218, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 28-218, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 24-370, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 146-398, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 146-398, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1464-1719, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-101, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-154, Full Length
Activity: Cell Activity

Expression system: E. coli
Length: 2-425, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 23-119, Partial
Activity: Not Tested

MMP3 is a member of the matrix metalloproteinase (MMP) family whose members are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, tissue remodeling, and disease processes including arthritis and metastasis. The MMP-3 enzyme degrades collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition, MMP-3 can also activate other MMPs such as MMP-1, MMP-7, and MMP-9, rendering MMP-3 crucial in connective tissue remodeling.[3] The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation.

Fcgr4, also known as CD16-2, is one of the receptors for Fc region of IgG which involve in immune responses. Fcgr4 mainly functions in cellular response to lipopolysaccharide, NK T cell proliferation, regulation of sensory perception of pain, wound healing etc. Three groups are included for Fc γ receptors (FcR), and they are Fc γ RI (CD64), Fc γ RII (CD32), and Fc γ RIII (CD16). Among these, CD64 possess high affinity even for monomeric IgG, while CD32 and CD16 display a relative lower affinity for IgG. Genes encodes these receptors are diverse differing by species and cell types. The aggregation of FcR having immunoreceptor tyrosine-based activation motifs (ITAMs) activates sequentially src family tyrosine kinases and syk family tyrosine kinases that connect transduced signals to common activation pathways shared with other receptors. FcR with ITAMs elicit cell activation, endocytosis, and phagocytosis. Fcgr4 belongs to Fc γ RIII (CD16) group.

Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is composed of just 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.

Expression system: E. coli
Length: 82-190, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 82-190, Full Length of Mature Protein
Activity: Cell Activity

Expression system: HEK293 Cells
Length: 279-390, Partial
Activity: Cell Activity

Expression system: HEK293 Cells
Length: 19-1170, Full Length of Mature Protein
Activity: Not Tested