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L4144

Sigma-Aldrich

Lectin from Phaseolus vulgaris (red kidney bean)

Leucoagglutinin PHA-L, lyophilized powder, BioReagent, suitable for cell culture

Synonym(s):

Phaseolus vulgaris agglutinin, PHA

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About This Item

EC Number:
UNSPSC Code:
12352202
NACRES:
NA.32

Quality Level

product line

BioReagent

form

lyophilized powder

potency

erythroagglutination activity (Does not agglutinate a 2% suspension of human erythrocytes at 250 μg lectin/ml.)
≤1.0 μg per mL leucoagglutination activity
≤5 μg per mL mitogenic activity (Bromdeoxyuridine incorporation in human peripheral blood mononuclear cells)

technique(s)

cell culture | mammalian: suitable

impurities

salt, free

solubility

DPBS: 5 mg/mL, slightly hazy, colorless

suitability

leucocyte agglutination activity tested

storage temp.

2-8°C

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General description

Lectins are carbohydrate-binding proteins, which contains four subunits with a molecular weight of 125 kDa. Leucoagglutinin PHA-L is a plant lectin, which is transported by the neurons in the central nervous system.

Application

Lectin from Phaseolus vulgaris (red kidney bean) has been used:
  • it has been used as a positive control to treat cells
  • to stimulate cell culture for the analysis of lymphocyte proliferation
  • to stimulate T cells

Biochem/physiol Actions

Lectin agglutinates cells and precipitates polysaccharides and glycoproteins. It is associated with toxic allergens and hemagglutinins. Lectin exhibits anti-cancer, anti-human immunodeficiency virus (anti-HIV) and anti-microbial infection properties. Lectin inhibits mucosal atrophy, lowers type 2 diabetes and obesity, enhances nutrient absorption and regulates drug targeting.
PHA consists of two molecular species, an erythroagglutinin (PHA-E) which has low mitogenic activity and high erythroagglutinin activity, and leucoagglutinin (PHA-L) which has high mitogenic and leucoagglutinating activity, but very low erythroagglutinating activity.
PHA-E is not blood group specific, but agglutination can be inhibited by certain oligosaccharides. PHA-P is the protein form of PHA prior to separation and purification of erythroagglutinin and leucoagglutinin. PHA-M is the mucoprotein form. Conjugates are prepared from the corresponding purified lectins.

Analysis Note

Agglutination activity is expressed in μg/ml and is determined from serial dilutions of a 1 mg/ml solution. This activity is the lowest concentration to agglutinate a suspension of either human erythrocytes (2% in phosphate buffered saline, pH 6.8) or human leukocytes (107 per mL in saline) after 1 hr incubation at 25 °C.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

动植物源性产品

Certificates of Analysis (COA)

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Haifeng Huang et al.
Acta pharmaceutica Sinica. B, 10(7), 1321-1330 (2020-09-03)
JS001 (toripalimab) is a humanized IgG monoclonal antibody which strongly inhibits programmed cell death protein 1 (PD1). In this study, we used a different iodine isotype (nat/124/125I) to label JS001 probes to target the human PD1 (hPD1) antigen. In vitro
Christopher Lai-Hipp et al.
Transfusion, 51(2), 333-337 (2010-08-28)
Cellular substrate (CS) composed of phytohemagglutinin (PHA)-stimulated PBMNCs is required for isolating primary human immunodeficiency virus Type 1 from plasma (PHIV) during early acute infection. The transmitted founder PHIV is neutralization-sensitive and uses chemokine-receptor 5 to infect CD4-positive PBMNCs. Therefore
SARS-CoV-2 vaccination in rituximab-treated patients: B cells promote humoral immune responses in the presence of T-cell-mediated immunity.
Mrak, et al.
Annals of the Rheumatic Diseases (2021)
Patricia Kaaijk et al.
Scientific reports, 11(1), 13664-13664 (2021-07-03)
Mumps is nowadays re-emerging despite vaccination. The contribution of T cell immunity to protection against mumps has not been clearly defined. Previously, we described a set of 41 peptides that were eluted from human leukocyte antigen (HLA) class I molecules
Benedikt Agerer et al.
Science immunology, 6(57) (2021-03-06)
CD8+ T cell immunity to SARS-CoV-2 has been implicated in COVID-19 severity and virus control. Here, we identified nonsynonymous mutations in MHC-I-restricted CD8+ T cell epitopes after deep sequencing of 747 SARS-CoV-2 virus isolates. Mutant peptides exhibited diminished or abrogated

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