Cytokines & Chemokines

Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. Cystatin-B / CSTB is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. Cystatin-B / CSTB is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. Cystatin-B / CSTB is also thought to play a role in protecting against the proteases leaking from lysosomes.

Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. Cystatin-B / CSTB is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. Cystatin-B / CSTB is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. Cystatin-B / CSTB is also thought to play a role in protecting against the proteases leaking from lysosomes.

IL-10, Rat,1mg

IL-10, Rat,100μg

CXCL11 also known as I-TAC is belonging to the CXC chemokine family and shares 36 % and 37 % amino acid sequence homology with IP-10 and MIG, respectively. It is highly expressed in peripheral blood leukocytes, pancreas and liver. Expression of CXCL11 is strongly induced by IFN-γ and IFN-β, and weakly induced by IFN-α. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3, which with a higher affinity than do the other chemokines for this receptor, CXCL9 and CXCL10. Similar to CXCL10, CXCL11 has been shown to be a chemoattractant for IL-2-activated T-lymphocytes, but not for isolated T-cells, neutrophils or monocytes.

CXCL11 also known as I-TAC is belonging to the CXC chemokine family and shares 36 % and 37 % amino acid sequence homology with IP-10 and MIG, respectively. It is highly expressed in peripheral blood leukocytes, pancreas and liver. Expression of CXCL11 is strongly induced by IFN-γ and IFN-β, and weakly induced by IFN-α. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3, which with a higher affinity than do the other chemokines for this receptor, CXCL9 and CXCL10. Similar to CXCL10, CXCL11 has been shown to be a chemoattractant for IL-2-activated T-lymphocytes, but not for isolated T-cells, neutrophils or monocytes.

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. It is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature rat EGF shares 70 % a.a. sequence identity with mature human EGF.

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. It is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature rat EGF shares 70 % a.a. sequence identity with mature human EGF.

Macrophage migration inhibitory factor (MIF or MMIF), also named as glycosylation-inhibiting factor (GIF), L-dopachrome isomerase, or phenylpyruvate tautomerase, is a protein encoded by the MIF gene. It is released from white blood cells by bacterial antigen stimulation to trigger an acute immune response, or by glucocorticoids to counter-act the inhibitory effects of glucocorticoids on immune system. MIF is a homotrimer of which each subunit contains 115 amino acids. As mentioned above, MIF is involved in the innate immune response to bacterial pathogens and counter-acts the anti-inflammatory activity of glucocorticoids. Furthermore, it also plays a role as mediator in regulating the function of macrophages in host defense and has phenylpyruvate tautomerase and dopachrome tautomerase activity in vitro. Mouse MIF is active on human cells, while human MIF is active on mouse cells. Mouse MIF is 99 %, 84 %, 90 %, and 90 % a.a. identical to rat, porcine, bovine and human MIF, respectively.