Product: C3 Antibody
Catalog: DF13224
Description: Rabbit polyclonal antibody to C3
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 187kDa; 187kD(Calculated).
Uniprot: P01024
RRID: AB_2846243

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
IF/ICC 1:100-1:500, WB 1:500-1:2000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Rabbit(88%), Dog(100%), Chicken(86%), Xenopus(80%)
Clonality:
Polyclonal
Specificity:
C3 Antibody detects endogenous levels of total C3.
RRID:
AB_2846243
Cite Format: Affinity Biosciences Cat# DF13224, RRID:AB_2846243.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

acylation-stimulating protein cleavage product; AHUS5; ARMD9; ASP; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1; C3; c3 complement; C3a anaphylatoxin; C3a; C3b; CO3_HUMAN; Complement C3; Complement C3c alpha' chain fragment 2; Complement C3c; Complement component 3; Complement component C3; Complement component C3a; Complement component C3b; Complement factor 3; CPAMD1; Prepro C3;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P01024 CO3_HUMAN:

Plasma. The acylation stimulating protein (ASP) is expressed in adipocytes and released into the plasma during both the fasting and postprandial periods.

Sequence:
MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAARRRRSVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACKKVFLDCCNYITELRRQHARASHLGLARSNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Bovine
100
Dog
100
Rabbit
88
Chicken
86
Xenopus
80
Horse
0
Sheep
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P01024 As Substrate

Site PTM Type Enzyme
S38 Phosphorylation
S70 Phosphorylation
N85 N-Glycosylation
S283 Phosphorylation
S287 Phosphorylation
K289 Ubiquitination
S297 Phosphorylation
S303 Phosphorylation
K305 Ubiquitination
S672 Phosphorylation
T676 Phosphorylation
Y686 Phosphorylation
S742 Phosphorylation
T885 Phosphorylation
S922 Phosphorylation
S928 Phosphorylation
N939 N-Glycosylation
S968 Phosphorylation
T1031 Phosphorylation
Y1194 Phosphorylation
S1315 Phosphorylation
S1321 Phosphorylation
T1341 Phosphorylation
S1343 Phosphorylation
Y1480 Phosphorylation
S1571 Phosphorylation
S1573 Phosphorylation
S1586 Phosphorylation
N1617 N-Glycosylation

Research Backgrounds

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. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.

Acts as a chemoattractant for neutrophils in chronic inflammation.

adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2.

PTMs:

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. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by insulin and dietary chylomicrons.

(Microbial infection) C3 is cleaved by Staphylococcus aureus aureolysin; this cleavage renders C3a and C3b inactive. C3b is rapidly degraded by host factors CFH and CFI preventing its deposition on the bacterial surface while C3a is further inactivated by aureolysin.

Phosphorylated by FAM20C in the extracellular medium.

Subcellular Location:

Secreted.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Plasma. The acylation stimulating protein (ASP) is expressed in adipocytes and released into the plasma during both the fasting and postprandial periods.

Subunit Structure:

C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). Forms the pro-C3-convertase enzyme complex by interacting with Complement factor B Bb fragment (Bb), which is then stabilized by binding CFP, allowing the complex to become active. The interaction with Bb is dependent on Mg2+. C3b interacts with CR1 (via Sushi 8 and Sushi 9 domains). C3b interacts with CFH. C3d interacts with CFH. C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). During pregnancy, C3dg exists as a complex (probably a 2:2:2 heterohexamer) with AGT and the proform of PRG2. Interacts with VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77.

(Microbial infection) C3b interacts with herpes simplex virus 1 (HHV-1) and herpes simplex virus 2 (HHV-2) envelope glycoprotein C; this interaction inhibits the activation of the complement system.

(Microbial infection) Interacts with Staphylococcus aureus immunoglobulin-binding protein Sbi; this interaction prevents the association between C3dg and CR2.

(Microbial infection) Interacts with Staphylococcus aureus protein Fib.

Research Fields

· Cellular Processes > Transport and catabolism > Phagosome.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Pertussis.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Parasitic > Leishmaniasis.

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

· Human Diseases > Infectious diseases: Bacterial > Staphylococcus aureus infection.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Cancers: Overview > Viral carcinogenesis.

· Human Diseases > Immune diseases > Systemic lupus erythematosus.

· Organismal Systems > Immune system > Complement and coagulation cascades.   (View pathway)

References

1). Remyelination-oriented clemastine treatment attenuates neuropathies of optic nerve and retina in glaucoma. Glia, 2024 (PubMed: 38829008) [IF=6.2]

2). Chronic spinal cord compression associated with intervertebral disc degeneration in SPARC-null mice. Neural Regeneration Research, 2023 (PubMed: 36018188) [IF=6.1]

Application: WB    Species: Mouse    Sample:

Figure 7 Astrocyte activation in L2/3 level in SPARC-null mice. (A–C) Immunofluorescence staining of GFAP with PCNA, C3, and S100A10. The expression of the astrocyte marker GFAP (green) was increased both in white and gray matter in SPARC-null mice compared with WT mice, PCNA, C3, and S100A10 (red) were significantly increased in SPARC-null mice. Scale bars: 500 µm in spinal cord overall view, 20 µm in gray and white matter. (D) Western blot and quantitative analysis of C3, S100A10, IL-10, and TGF-β (normalized to β-actin). Data are shown as mean ± SD (n = 3 mice in each group). **P < 0.01, ***P < 0.001 (Student’s t-test). C3: Complement component 3; GFAP: glial fibrillary acidic protein; IL-10: interleukin-10; PCNA: proliferating cell nuclear antigen; S100A10: soluble protein-100α10; SPARC: secreted protein, acidic and rich in cysteine; TGF-β: transforming growth factor-beta; WT: wild-type.

Application: IF/ICC    Species: Mouse    Sample:

Figure 7 Astrocyte activation in L2/3 level in SPARC-null mice. (A–C) Immunofluorescence staining of GFAP with PCNA, C3, and S100A10. The expression of the astrocyte marker GFAP (green) was increased both in white and gray matter in SPARC-null mice compared with WT mice, PCNA, C3, and S100A10 (red) were significantly increased in SPARC-null mice. Scale bars: 500 µm in spinal cord overall view, 20 µm in gray and white matter. (D) Western blot and quantitative analysis of C3, S100A10, IL-10, and TGF-β (normalized to β-actin). Data are shown as mean ± SD (n = 3 mice in each group). **P < 0.01, ***P < 0.001 (Student’s t-test). C3: Complement component 3; GFAP: glial fibrillary acidic protein; IL-10: interleukin-10; PCNA: proliferating cell nuclear antigen; S100A10: soluble protein-100α10; SPARC: secreted protein, acidic and rich in cysteine; TGF-β: transforming growth factor-beta; WT: wild-type.

3). Inhibition of HDAC6 alleviates cancer‑induced bone pain by reducing the activation of NLRP3 inflammasome. International journal of molecular medicine, 2024 (PubMed: 37997785) [IF=5.4]

Application: WB    Species: Rat    Sample: spinal cord

Figure 4 Effect of TSA on the spinal astrocytic activation. Representative immunofluorescence staining images (A) and quantitative analysis (B) for GFAP and CFB in the spinal cord. Scale bar, 20 μm. Representative western blot bands (C) and quantitative analysis (D) of GFAP, C3 and CFB proteins in the spinal cord. Data were presented as mean ± SD (n=3). *P

4). C‐reactive protein inhibits C3a/C3aR‐dependent podocyte autophagy in favor of diabetic kidney disease. The FASEB Journal, 2022 (PubMed: 35503088) [IF=4.8]

5). Daphnetin Improves Neuropathic Pain by Inhibiting the Expression of Chemokines and Inflammatory Factors in the Spinal Cord and Interfering with Glial Cell Polarization. Pharmaceuticals, 2023 (PubMed: 37259390) [IF=4.6]

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