Human Serum Albumin Antibody [L7A9]

Application: Reactivity: Human

Usage Information

Dilution
WB1:2000-1:10000 IHC1:80-1:20000 IF1:80-1:250 FCM1:8000

Application
WB, IHC, IF, FCM

Reactivity
Human

Source
Mouse 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
69 kDa 65-70 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	Human liver tissue; Human serum; BG01V human embryonic stem cells differentiated to hepatocytes; HepG2 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Human Serum Albumin Antibody [L7A9] detects endogenous levels of total Human Serum Albumin protein.

Clone
L7A9

Synonym(s)
ALB

Background
Human Serum Albumin, or HSA, is the most abundant globular protein in blood plasma. It is a non-glycosylated member of the albumin protein family, synthesized primarily in the liver by hepatocytes, and forms a heart-shaped molecule that is predominantly alpha-helical, with approximately 67 percent of its structure composed of alpha helices. It is organized into three homologous domains: domain I spans residues 1 to 195, domain II from 196 to 383, and domain III from 384 to 585. Each domain is further divided into subdomains A, which contains six helices, and B, which contains four helices, and the protein is stabilized by 17 intramolecular disulfide bonds that pair 34 cysteine residues, leaving Cys34 as a free thiol. The principal ligand-binding sites, known as Sudlow site I in subdomain IIA and Sudlow site II in subdomain IIIA, accommodate a wide range of ligands including fatty acids, hormones, bilirubin, metal ions, and numerous drugs. HSA is essential for maintaining colloidal osmotic pressure, accounting for about 80 percent of plasma oncotic pressure, thus regulating vascular volume and capillary permeability. It serves as a bidirectional carrier, transporting hydrophobic ligands such as fatty acids. There are seven high-affinity binding sites: heme, thyroxine, and various drugs, from tissues to sites of metabolism or excretion. HSA also scavenges reactive oxygen species and neutralizes toxins via its Cys34 thiol group, and it plays a role in modulating neutrophil adhesion and inflammation. HSA is crucial for nutrient delivery, influences drug pharmacokinetics by prolonging half-life and altering distribution, and provides antioxidant defense, accounting for roughly 80 percent of the plasma's antioxidant capacity. Low levels of HSA, a condition known as hypoalbuminemia, are associated with edema, liver disease, and malnutrition, while structural modifications such as oxidation and glycation can impair its function, as seen in diabetes and critical illness.

Background

Human Serum Albumin, or HSA, is the most abundant globular protein in blood plasma. It is a non-glycosylated member of the albumin protein family, synthesized primarily in the liver by hepatocytes, and forms a heart-shaped molecule that is predominantly alpha-helical, with approximately 67 percent of its structure composed of alpha helices. It is organized into three homologous domains: domain I spans residues 1 to 195, domain II from 196 to 383, and domain III from 384 to 585. Each domain is further divided into subdomains A, which contains six helices, and B, which contains four helices, and the protein is stabilized by 17 intramolecular disulfide bonds that pair 34 cysteine residues, leaving Cys34 as a free thiol. The principal ligand-binding sites, known as Sudlow site I in subdomain IIA and Sudlow site II in subdomain IIIA, accommodate a wide range of ligands including fatty acids, hormones, bilirubin, metal ions, and numerous drugs. HSA is essential for maintaining colloidal osmotic pressure, accounting for about 80 percent of plasma oncotic pressure, thus regulating vascular volume and capillary permeability. It serves as a bidirectional carrier, transporting hydrophobic ligands such as fatty acids. There are seven high-affinity binding sites: heme, thyroxine, and various drugs, from tissues to sites of metabolism or excretion. HSA also scavenges reactive oxygen species and neutralizes toxins via its Cys34 thiol group, and it plays a role in modulating neutrophil adhesion and inflammation. HSA is crucial for nutrient delivery, influences drug pharmacokinetics by prolonging half-life and altering distribution, and provides antioxidant defense, accounting for roughly 80 percent of the plasma's antioxidant capacity. Low levels of HSA, a condition known as hypoalbuminemia, are associated with edema, liver disease, and malnutrition, while structural modifications such as oxidation and glycation can impair its function, as seen in diabetes and critical illness.

References
https://pubmed.ncbi.nlm.nih.gov/38111902/ https://pubmed.ncbi.nlm.nih.gov/25732553/

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%