C4 binding protein/C4BPB Antibody [K15D12]

Application: Reactivity: Rat, Human

Usage Information

Dilution
WB1:1000 IP1:80 IHC1:1000 IF1:250

Application
WB, IP, IHC, IF

Reactivity
Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
28,37,73 kDa 42,45,73 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Rat liver tissue; Human bladder carcinoma tissue; Human hepatocellular carcinoma tissue; Human ovary cancer; Rat plasma; Human serum; HepG2 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
C4 binding protein/C4BPB Antibody [K15D12] detects endogenous levels of total C4 binding protein/C4BPB protein.

Clone
K15D12

Synonym(s)
C4b-binding protein beta chain; C4BPB

Background
C4b-binding protein (C4BP), including its beta-chain C4BPB, is a key soluble regulator of the classical and lectin complement pathways, mainly produced in the liver as a large glycoprotein complex made up of seven alpha-chains, each with eight complement control protein domains, and one beta-chain with three such domains, linked by disulfide bonds at their C-termini to form a spider-like structure. The alpha-chain domains one to three bind C4b to inhibit C3 convertase (C4b2a) formation, act as a cofactor for Factor I to cleave C4b into inactive C4c and C4d, and speed up C2a dissociation, thereby preventing excessive complement activation, while the beta-chain links with Protein S to help balance anticoagulation. As an acute-phase protein, C4BP is upregulated fourfold during inflammation (favoring the alpha-seven-beta-zero isoform), limits tissue damage, promotes apoptotic cell clearance via Protein S, and modulates the NLRP3 inflammasome to reduce interleukin-1 beta in conditions like diabetes and gout, but can also be hijacked by pathogens such as Neisseria or Streptococcus and by tumors for immune evasion and increased survival. C4BP binds to CD40 to promote B-cell proliferation and survival, inhibits apoptosis in cholangiocytes, and is involved in diseases including systemic lupus erythematosus (where beta-chain-lacking C4BP protects the kidneys), rheumatoid arthritis (through DNA binding), and various cancers, where it may support anti-tumour immunity or protect cancer cells. The beta-chain C4BPB uniquely binds to Protein S at a hydrophobic site in its first domain, stabilising approximately seventy per cent of plasma Protein S for coagulation homeostasis, a process that can become dysregulated during inflammation.

Background

C4b-binding protein (C4BP), including its beta-chain C4BPB, is a key soluble regulator of the classical and lectin complement pathways, mainly produced in the liver as a large glycoprotein complex made up of seven alpha-chains, each with eight complement control protein domains, and one beta-chain with three such domains, linked by disulfide bonds at their C-termini to form a spider-like structure. The alpha-chain domains one to three bind C4b to inhibit C3 convertase (C4b2a) formation, act as a cofactor for Factor I to cleave C4b into inactive C4c and C4d, and speed up C2a dissociation, thereby preventing excessive complement activation, while the beta-chain links with Protein S to help balance anticoagulation. As an acute-phase protein, C4BP is upregulated fourfold during inflammation (favoring the alpha-seven-beta-zero isoform), limits tissue damage, promotes apoptotic cell clearance via Protein S, and modulates the NLRP3 inflammasome to reduce interleukin-1 beta in conditions like diabetes and gout, but can also be hijacked by pathogens such as Neisseria or Streptococcus and by tumors for immune evasion and increased survival. C4BP binds to CD40 to promote B-cell proliferation and survival, inhibits apoptosis in cholangiocytes, and is involved in diseases including systemic lupus erythematosus (where beta-chain-lacking C4BP protects the kidneys), rheumatoid arthritis (through DNA binding), and various cancers, where it may support anti-tumour immunity or protect cancer cells. The beta-chain C4BPB uniquely binds to Protein S at a hydrophobic site in its first domain, stabilising approximately seventy per cent of plasma Protein S for coagulation homeostasis, a process that can become dysregulated during inflammation.

References
https://pubmed.ncbi.nlm.nih.gov/10329721/ https://pubmed.ncbi.nlm.nih.gov/35547734/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%