Product Name: ALB Antibody (biotin)
Species Reactivity: Human
Tested Applications: ELISA, IHC, WB
Applications: ALB antibody can be used in ELISA starting at 1:400 – 1:1600, Western Blot, and immunohistochemistry starting at 10 μg/mL.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight:
Immunogen: ALB antibody was raised against amino acids 359 – 368 of ALB (Human).
Host Species: Rabbit
Purification: Immunoaffinity Chromatography
Physical State: Liquid
CAS NO.: 133718-30-6
Product: R 80123
Buffer: 0.02 M potassium phosphate, 0.15 M sodium chloride, pH 7.2, 10 mg/mL BSA (IgG, protease free), 0.01% sodium azide.
Concentration:
Storage Conditions: Store ALB antibody at 4 ˚C or -20 ˚C. As with all antibodies avoid freeze/thaw cycles.
Clonality: Polyclonal
Conjugate: Biotin
Alternate Names: ALB, Albumin (32 AA), Albumin (AA 34), Albumin, Growth-inhibiting protein 20, PRO1341, PRO0883, Serum albumin, PRO0903
Accession NO.: P02768
Protein Ino: 113576
Official Symbol: ALB
Geneid: 213
Background: Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in the ALB gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative cap site to the first poly(A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain. Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to give the secreted albumin.
PubMed ID:http://aac.asm.org/content/52/8/2727.abstract
