Overview

Description

  • Nature
    Synthetic
  • Source
    Synthetic
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      Biotin-SVQLTEKRMD KVGKYPKELR KCCEDGMREN PMRFSCQRRT RFISLGEACK KVFLDCCNYI TELRRQHARA SHLGLAR
    • Molecular weight
      9 kDa
    • Amino acids
      672 to 748
    • Additional sequence information
      The sequence refers to the C3a anaphylatoxin chain.
  • Conjugation
    Biotin

Specifications

Our Abpromise guarantee covers the use of ab176059 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    HPLC

  • Form
    Lyophilised
  • Additional notes

    Biotin incorporated at indicated position in a molar ratio of biotin:peptide of 1:1.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    Information available upon request.

  • Reconstitution
    It is recommended vials be centrifuged prior to opening. Water can be used to prepare stock solutions of 20 µmol.L-1. Stock solutions with up to 30% DMSO/water can also be prepared.

General Info

  • Alternative names
    • Acylation stimulating protein cleavage product
    • AHUS5
    • ARMD9
    • ASP
    • C3
    • C3 and PZP like alpha 2 macroglobulin domain containing protein 1
    • C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1
    • c3 complement
    • CO3_HUMAN
    • Complement C3
    • Complement C3c alpha'' chain fragment 2
    • Complement component 3
    • Complement factor 3
    • CPAMD1
    • HEL S 62p
    see all
  • Function
    C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.
    Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.
  • Tissue specificity
    Plasma.
  • Involvement in disease
    Defects in C3 are the cause of complement component 3 deficiency (C3D) [MIM:120700]. A rare defect of the complement classical pathway. Patients develop recurrent, severe, pyogenic infections because of ineffective opsonization of pathogens. Some patients may also develop autoimmune disorders, such as arthralgia and vasculitic rashes, lupus-like syndrome and membranoproliferative glomerulonephritis.
    Genetic variation in C3 is associated with susceptibility to age-related macular degeneration type 9 (ARMD9) [MIM:611378]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
    Defects in C3 are a cause of susceptibility to hemolytic uremic syndrome atypical type 5 (AHUS5) [MIM:612925]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.
  • Sequence similarities
    Contains 1 anaphylatoxin-like domain.
    Contains 1 NTR domain.
  • Post-translational
    modifications
    C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g.
    Phosphorylation sites are present in the extracelllular medium.
  • Cellular localization
    Secreted.
  • Information by UniProt

References

ab176059 has not yet been referenced specifically in any publications.

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