protein

Human Complement Component C3c

MBS143106

0.2 mg

140 USD

Native Protein

Human Complement Component C3c

Complement Component C3c

C3c Human; Complement Component C3c Human; Complement C3c; Complement Component C3c; C3c

complement component c3a, duplicate 3; complement component c3a, duplicate 3; c3.3; complement component C3-2; complement component c3c; complement component c3a, duplicate 3

C3c

c3a.3; c3c; C3-3; c3-2; unp301; zgc:103610

Human Plasma

1651

Greater than 96.0%.

The Human Complement C3c was lyophilized in a sodium phosphate buffer, pH 7.2, containing 0.15M NaCl. Sterile Filtered White lyophilized (freeze-dried) powder.

Human C3c although stable at room temperature for 3 weeks, should be stored between 2-8 degree C.

Solubility: It is recommended to reconstitute the lyophilized C3c in de-ionized water. Human Virus Test: Plasma from each donor has been tested and found negative for HIV-1 & 2 antibodies, Hepatatis B surface antigen, and Hepatatis C antibodies.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins; Complement Component

Description: Human C3c produced in Human Plasma having a molecular mass of 137 KDa. Introduction: The C3c component is central in both complement activation pathways, with different specific proteolytic systems cleaving it to form C3 convertase. Cleavage of C3 releases C3a and the C3b fragment which is part of the alternative C3 convertase. C3 levels can be low because of decreased synthesis or due to consumption. High C3 levels are seen in highly acute or chronic inflammation, hepatic cholestasis and during the third trimester of pregnancy.Unwanted complement activation is a major cause of tissue damage in various pathological conditions and contributes to quite a few immune complex diseases. Compstatin is an effective inhibitor of the activation of complement component C3 and thus blocks a central and essential step in the complement cascade. The specific binding site on C3, the configuration in the bound form, and the exact mode of action of compstatin are unknown. The crystal structure of compstatin in complex with C3c reveals that the compstatin-binding site is formed by the macroglobulin (MG) domains 4 and 5. This binding site is part of the structurally stable MG-ring created by domains MG16 and is distant from any other known binding site on C3. Compstatin does not modify the conformation of C3c, while compstatin itself undergoes a large conformational alteration upon binding.

82524318

NP_001032313.1

NM_001037236.1

Activation Of C3 And C5 Pathway (1114768); Alternative Complement Activation Pathway (1114767); Class A/1 (Rhodopsin-like Receptors) Pathway (1113813); Complement Cascade Pathway (1114763); Defective ACTH Causes Obesity And Pro-opiomelanocortinin Deficiency (POMCD) Pathway (1114596); Disease Pathway (1114410); G Alpha (i) Signalling Events Pathway (1113844); GPCR Downstream Signaling Pathway (1113842); GPCR Ligand Binding Pathway (1113812); Herpes Simplex Infection Pathway (377867)

0.2 mg

140 USD

1 mg

205

10 mg

1125