human c5a elisa kit Search Results


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Hycult Biotech c5a
C5a, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Sino Biological c5a elisa kit
C5a Elisa Kit, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Elabscience Biotechnology c5a
Figure 2: Te concentrations of complement pyrolysis products were found higher in pleural efusion than in plasma from TPE patients. (a) Complement pyrolysis products, including C3a, C3b, C3d, <t>C5a,</t> and opsonin receptors (CR1 and CR3) were detected in human tuberculosis pleural biopsy samples by immunohistochemistry. (Original magnifcation, ×200) (n 4). (b) Higher levels of complement pyrolysis products were found in pleural efusion than in plasma in TPE patients (n 20). Te concentrations of complement pyrolysis products in pleural fuid and plasma from TPE patients were measured by ELISA (n 20).
C5a, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cusabio human c5a elisa kit
C. trachomatis infection yielded a novel undescribed C5 fragment independent of C3. (A) C . trachomatis -HeLa229 cell lysates (MOI=1) incubated with human purified C5 (400 nM) produced a previously undescribed ~38-kDa fragment encompassing <t>C5a</t> in Western blot analysis. (B) Schematic overview of proteolytical processing of C5 induced by traditional C5 convertases or C . trachomatis infection. (C) C . trachomatis infection generated a limited amount of C5a in the absence of C3 detected by <t>ELISA.</t> The C5 control group was taken as the baseline. Formation rates of C5a were calculated according to the concentration of human C5 protein before the reaction (400 nM). ns, not significant; *P < 0.05; **P < 0.01; ****P < 0.0001 (Dunnett’s multiple comparisons test, n =3).
Human C5a Elisa Kit, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson human c3a elisa kit
C. trachomatis infection yielded a novel undescribed C5 fragment independent of C3. (A) C . trachomatis -HeLa229 cell lysates (MOI=1) incubated with human purified C5 (400 nM) produced a previously undescribed ~38-kDa fragment encompassing <t>C5a</t> in Western blot analysis. (B) Schematic overview of proteolytical processing of C5 induced by traditional C5 convertases or C . trachomatis infection. (C) C . trachomatis infection generated a limited amount of C5a in the absence of C3 detected by <t>ELISA.</t> The C5 control group was taken as the baseline. Formation rates of C5a were calculated according to the concentration of human C5 protein before the reaction (400 nM). ns, not significant; *P < 0.05; **P < 0.01; ****P < 0.0001 (Dunnett’s multiple comparisons test, n =3).
Human C3a Elisa Kit, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson mouse recombinant c3a c5a
C. trachomatis infection yielded a novel undescribed C5 fragment independent of C3. (A) C . trachomatis -HeLa229 cell lysates (MOI=1) incubated with human purified C5 (400 nM) produced a previously undescribed ~38-kDa fragment encompassing <t>C5a</t> in Western blot analysis. (B) Schematic overview of proteolytical processing of C5 induced by traditional C5 convertases or C . trachomatis infection. (C) C . trachomatis infection generated a limited amount of C5a in the absence of C3 detected by <t>ELISA.</t> The C5 control group was taken as the baseline. Formation rates of C5a were calculated according to the concentration of human C5 protein before the reaction (400 nM). ns, not significant; *P < 0.05; **P < 0.01; ****P < 0.0001 (Dunnett’s multiple comparisons test, n =3).
Mouse Recombinant C3a C5a, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson human c5a elisa kit ii bd opteiatm
C. trachomatis infection yielded a novel undescribed C5 fragment independent of C3. (A) C . trachomatis -HeLa229 cell lysates (MOI=1) incubated with human purified C5 (400 nM) produced a previously undescribed ~38-kDa fragment encompassing <t>C5a</t> in Western blot analysis. (B) Schematic overview of proteolytical processing of C5 induced by traditional C5 convertases or C . trachomatis infection. (C) C . trachomatis infection generated a limited amount of C5a in the absence of C3 detected by <t>ELISA.</t> The C5 control group was taken as the baseline. Formation rates of C5a were calculated according to the concentration of human C5 protein before the reaction (400 nM). ns, not significant; *P < 0.05; **P < 0.01; ****P < 0.0001 (Dunnett’s multiple comparisons test, n =3).
Human C5a Elisa Kit Ii Bd Opteiatm, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Techne corporation human complement component c5a duoset elisa
C. trachomatis infection yielded a novel undescribed C5 fragment independent of C3. (A) C . trachomatis -HeLa229 cell lysates (MOI=1) incubated with human purified C5 (400 nM) produced a previously undescribed ~38-kDa fragment encompassing <t>C5a</t> in Western blot analysis. (B) Schematic overview of proteolytical processing of C5 induced by traditional C5 convertases or C . trachomatis infection. (C) C . trachomatis infection generated a limited amount of C5a in the absence of C3 detected by <t>ELISA.</t> The C5 control group was taken as the baseline. Formation rates of C5a were calculated according to the concentration of human C5 protein before the reaction (400 nM). ns, not significant; *P < 0.05; **P < 0.01; ****P < 0.0001 (Dunnett’s multiple comparisons test, n =3).
Human Complement Component C5a Duoset Elisa, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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N/A
C5a is a protein fragment released from cleavage complement component C5 by protease C5-convertase into C5a and C5b fragments. C5b is important in late events of complement cascade, whereas C5a acts as highly inflammatory peptide.The
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N/A
An ELISA kit for the detection of C5a Human This uses Sandwich ELISA Double Antibody and has a sensitivity of 46 875pg ml
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N/A
Activation of the classical alternate or lectin complement pathways can result in the production of the C5a anaphylatoxin C5a is a multifunctional proinflammatory mediator Thus C5a has been observed to increase vascular permeability to be
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Image Search Results


Figure 2: Te concentrations of complement pyrolysis products were found higher in pleural efusion than in plasma from TPE patients. (a) Complement pyrolysis products, including C3a, C3b, C3d, C5a, and opsonin receptors (CR1 and CR3) were detected in human tuberculosis pleural biopsy samples by immunohistochemistry. (Original magnifcation, ×200) (n 4). (b) Higher levels of complement pyrolysis products were found in pleural efusion than in plasma in TPE patients (n 20). Te concentrations of complement pyrolysis products in pleural fuid and plasma from TPE patients were measured by ELISA (n 20).

Journal: International Journal of Clinical Practice

Article Title: Pleural Mesothelial Cells-Induced Monocytes to the Pleural Cavity through the Effect of C3 Lytic Products in Tuberculous Pleural Effusion

doi: 10.1155/2024/5544085

Figure Lengend Snippet: Figure 2: Te concentrations of complement pyrolysis products were found higher in pleural efusion than in plasma from TPE patients. (a) Complement pyrolysis products, including C3a, C3b, C3d, C5a, and opsonin receptors (CR1 and CR3) were detected in human tuberculosis pleural biopsy samples by immunohistochemistry. (Original magnifcation, ×200) (n 4). (b) Higher levels of complement pyrolysis products were found in pleural efusion than in plasma in TPE patients (n 20). Te concentrations of complement pyrolysis products in pleural fuid and plasma from TPE patients were measured by ELISA (n 20).

Article Snippet: Te concentrations of complement components and chemokines, including C1q (E-EL-H6053), factor B (E-ELH6056), factor (E-EL-H0817), MBL (E-EL-H1305), MAC (E-EL-H2376), CD46 (ab283877, Abcam), C3 (E-ELH6054), C5 (E-EL-H0810), C3a (E-EL-H0818), C5a (E-ELH0190), C3b (E-EL-H6054), C3d (E-EL-H5457), and CXCL12 (E-EL-H0052c), in both pleural fuids and plasma were measured by ELISA kits according to the manufacturer’s protocols (all kits were purchased from Elabscience and Abcam).

Techniques: Clinical Proteomics, Immunohistochemistry, Enzyme-linked Immunosorbent Assay

C. trachomatis infection yielded a novel undescribed C5 fragment independent of C3. (A) C . trachomatis -HeLa229 cell lysates (MOI=1) incubated with human purified C5 (400 nM) produced a previously undescribed ~38-kDa fragment encompassing C5a in Western blot analysis. (B) Schematic overview of proteolytical processing of C5 induced by traditional C5 convertases or C . trachomatis infection. (C) C . trachomatis infection generated a limited amount of C5a in the absence of C3 detected by ELISA. The C5 control group was taken as the baseline. Formation rates of C5a were calculated according to the concentration of human C5 protein before the reaction (400 nM). ns, not significant; *P < 0.05; **P < 0.01; ****P < 0.0001 (Dunnett’s multiple comparisons test, n =3).

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: A Novel Cleavage Pattern of Complement C5 Induced by Chlamydia trachomatis Infection via the Chlamydial Protease CPAF

doi: 10.3389/fcimb.2021.732163

Figure Lengend Snippet: C. trachomatis infection yielded a novel undescribed C5 fragment independent of C3. (A) C . trachomatis -HeLa229 cell lysates (MOI=1) incubated with human purified C5 (400 nM) produced a previously undescribed ~38-kDa fragment encompassing C5a in Western blot analysis. (B) Schematic overview of proteolytical processing of C5 induced by traditional C5 convertases or C . trachomatis infection. (C) C . trachomatis infection generated a limited amount of C5a in the absence of C3 detected by ELISA. The C5 control group was taken as the baseline. Formation rates of C5a were calculated according to the concentration of human C5 protein before the reaction (400 nM). ns, not significant; *P < 0.05; **P < 0.01; ****P < 0.0001 (Dunnett’s multiple comparisons test, n =3).

Article Snippet: Quantitative analysis of C5a in the cleavage products were analyzed using a commercially available human C5a ELISA kit (CUSABIO BIOTECH, Wuhan, China) according to the manufacturer’s instructions.

Techniques: Infection, Incubation, Purification, Produced, Western Blot, Generated, Enzyme-linked Immunosorbent Assay, Control, Concentration Assay

Chlamydial infection after 24 hours post-infection but not EB cleaves C5 at K970 site. (A) The (C) trachomatis-HeLa229 cell lysates (MOI=1) collected at 0 h, 12 h, 24 h, 36h and 44 h post-infection were co-incubated with purified C5 (400 nM) for 120 min. Western blot analysis showed the fragments encompassing C5a. (B) The purified chlamydial EBs were co-incubated with purified C5 (400 nM) for 30 min. Western blot analysis showed the fragments encompassing C5a. (C) Penicillin treatment significantly reduced the consumption of the band of C5α chain, and also inhibited the expression of CPAF.

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: A Novel Cleavage Pattern of Complement C5 Induced by Chlamydia trachomatis Infection via the Chlamydial Protease CPAF

doi: 10.3389/fcimb.2021.732163

Figure Lengend Snippet: Chlamydial infection after 24 hours post-infection but not EB cleaves C5 at K970 site. (A) The (C) trachomatis-HeLa229 cell lysates (MOI=1) collected at 0 h, 12 h, 24 h, 36h and 44 h post-infection were co-incubated with purified C5 (400 nM) for 120 min. Western blot analysis showed the fragments encompassing C5a. (B) The purified chlamydial EBs were co-incubated with purified C5 (400 nM) for 30 min. Western blot analysis showed the fragments encompassing C5a. (C) Penicillin treatment significantly reduced the consumption of the band of C5α chain, and also inhibited the expression of CPAF.

Article Snippet: Quantitative analysis of C5a in the cleavage products were analyzed using a commercially available human C5a ELISA kit (CUSABIO BIOTECH, Wuhan, China) according to the manufacturer’s instructions.

Techniques: Infection, Incubation, Purification, Western Blot, Expressing

CPAF induces a C5-derived novel fragment independent of C3. (A) Purified C5 was incubated with PBS, HeLa229 cells lysate, C . trachomatis -HeLa229 cells lysate, or C . trachomatis CPAF −/− -HeLa229 cells lysate, respectively. Products of the incubation were subjected to immunoblot analysis against C5a, MOMP, and CPAFc. (B) Lactacystin (500 μM) failed to inhibit C5 cleavage induced by 1:1 dilution of C. trachomatis -HeLa229 cell lysates, but slightly reduced consumption of the band corresponding to the C5α chain (115 kDa) in the group of 1:2 dilution of C. trachomatis -HeLa229 cell lysates.

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: A Novel Cleavage Pattern of Complement C5 Induced by Chlamydia trachomatis Infection via the Chlamydial Protease CPAF

doi: 10.3389/fcimb.2021.732163

Figure Lengend Snippet: CPAF induces a C5-derived novel fragment independent of C3. (A) Purified C5 was incubated with PBS, HeLa229 cells lysate, C . trachomatis -HeLa229 cells lysate, or C . trachomatis CPAF −/− -HeLa229 cells lysate, respectively. Products of the incubation were subjected to immunoblot analysis against C5a, MOMP, and CPAFc. (B) Lactacystin (500 μM) failed to inhibit C5 cleavage induced by 1:1 dilution of C. trachomatis -HeLa229 cell lysates, but slightly reduced consumption of the band corresponding to the C5α chain (115 kDa) in the group of 1:2 dilution of C. trachomatis -HeLa229 cell lysates.

Article Snippet: Quantitative analysis of C5a in the cleavage products were analyzed using a commercially available human C5a ELISA kit (CUSABIO BIOTECH, Wuhan, China) according to the manufacturer’s instructions.

Techniques: Derivative Assay, Purification, Incubation, Western Blot

NM inhibits the C3-independent C5 activation triggered by chlamydial infection and has a reasonable inhibitory conformation with CPAF. (A) NM (400 μM) was pre-mixed with different dilutions of C . trachomatis -HeLa229 cell lysates. Purified C5 was then incubated with PBS or the C . trachomatis -HeLa229 cell lysates for 30 min, respectively. The resulting products were subjected to immunoblot analysis against C5a, MOMP, and CPAFc. (B) The 3D structure of NM-CPAF complex. (C) The surface of the active site of CPAF. (D) The detail binding mode of NM-CPAF complex. The backbone of CPAF was rendered in tube and colored in bright blue. NM was colored in yellow. The hydrogen bonds in NM-CPAF complex were shown in red dashed lines.

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: A Novel Cleavage Pattern of Complement C5 Induced by Chlamydia trachomatis Infection via the Chlamydial Protease CPAF

doi: 10.3389/fcimb.2021.732163

Figure Lengend Snippet: NM inhibits the C3-independent C5 activation triggered by chlamydial infection and has a reasonable inhibitory conformation with CPAF. (A) NM (400 μM) was pre-mixed with different dilutions of C . trachomatis -HeLa229 cell lysates. Purified C5 was then incubated with PBS or the C . trachomatis -HeLa229 cell lysates for 30 min, respectively. The resulting products were subjected to immunoblot analysis against C5a, MOMP, and CPAFc. (B) The 3D structure of NM-CPAF complex. (C) The surface of the active site of CPAF. (D) The detail binding mode of NM-CPAF complex. The backbone of CPAF was rendered in tube and colored in bright blue. NM was colored in yellow. The hydrogen bonds in NM-CPAF complex were shown in red dashed lines.

Article Snippet: Quantitative analysis of C5a in the cleavage products were analyzed using a commercially available human C5a ELISA kit (CUSABIO BIOTECH, Wuhan, China) according to the manufacturer’s instructions.

Techniques: Activation Assay, Infection, Purification, Incubation, Western Blot, Binding Assay