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Manufactured by BioVendor

Bile Salt-Activated Lipase NATIVE, Human Breast Milk

  • Regulatory status:RUO
  • Type:Native protein
  • Source:Human breast milk
  • Other names:BAL, Bile salt-stimulated lipase, BSSL, Bucelipase, Carboxyl ester lipase, Cholesterol esterase, Pancreatic lysophospholipase, Sterol esterase, CEL
  • Species:Human
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Cat. No. Size Price

RD166341050 0.05 mg
PubMed Product Details
Technical Data


Native protein


Native protein isolated from Human Breast Milk, 733 AA, MW 79,322 kDa (calculated without glycosylation). Protein identity confirmed by LC-MS/MS (NCBI no. gi|27769331).

Amino Acid Sequence



Human breast milk


Purity as determined by densitometric image analysis: >95%


SDS-PAGE analysis of Bile salt-activated lipase NATIVE protein, 12% gel stained with Coomassie Brillant Blue G250

  1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
  2. reduced and boiled sample, 2.5ug/lane
  3. non-reduced and non-boiled sample, 2.5μg/lane


< 1.0 EU/ug


Filtered (0,4 μm) and lyophilized in 0.5 mg/mL in 0,05M phosphate buffer, 0,075M NaCl, pH 7,4.


Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.


Western blotting, ELISA, Cell culture and/or animal studies, Immunological methods


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.
LC-MS/MS to identify the protein and determine purity of the protein.
SDS PAGE to determine purity of the protein.
LAL to determine quantity of endotoxin.


This product is intended for research use only.


Research topic



Bile salt-activated lipase (BAL) is one of two lipases secreted from the vertebrate pancreas into the intestine for the digestion of fat. There is evidence to support the importance of bile salt-activated lipase for the absorption of cholesterol, vitamin A and triacylglycerol. In mammals, including humans, BAL is also present in the milk to facilitate fat absorption in infants. Human breast milk contains a bile salt activated lipase at a very high level. The human milk bile salt-activated lipase has also been shown to be identical to bile salt-dependent lipase (BSDL), that is produced in pancreas and has been also documented with several different names, including pancreatic carboxyl ester lipase, pancreatic cholesterol esterase, triacylglycerol lipase, and lysophospholipase.

Summary References (13)

References to Bile Salt-Activated Lipase

  • Baba T, Downs D, Jackson KW, Tang J, Wang CS. Structure of human milk bile salt activated lipase. Biochemistry. 1991 Jan 15;30 (2):500-10
  • Christie DL, Cleverly DR, O'Connor CJ. Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. FEBS Lett. 1991 Jan 28;278 (2):190-4
  • Hui DY, Hayakawa K, Oizumi J. Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase). Biochem J. 1993 Apr 1;291 ( Pt 1):65-9
  • Hui DY, Kissel JA. Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 1990 Dec 10;276 (1-2):131-4
  • Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM,. DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429 (6990):369-74
  • Lidberg U, Nilsson J, Stromberg K, Stenman G, Sahlin P, Enerback S, Bjursell G. Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomics. 1992 Jul;13 (3):630-40
  • Madeyski K, Lidberg U, Bjursell G, Nilsson J. Structure and organization of the human carboxyl ester lipase locus. Mamm Genome. 1998 Apr;9 (4):334-8
  • Mechref Y, Chen P, Novotny MV. Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk. Glycobiology. 1999 Mar;9 (3):227-34
  • Nilsson J, Blackberg L, Carlsson P, Enerback S, Hernell O, Bjursell G. cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur J Biochem. 1990 Sep 11;192 (2):543-50
  • Raeder H, Johansson S, Holm PI, Haldorsen IS, Mas E, Sbarra V, Nermoen I, Eide SA, Grevle L, Bjorkhaug L, Sagen JV, Aksnes L, Sovik O, Lombardo D, Molven A, Njolstad PR. Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction. Nat Genet. 2006 Jan;38 (1):54-62
  • Roudani S, Miralles F, Margotat A, Escribano MJ, Lombardo D. Bile salt-dependent lipase transcripts in human fetal tissues. Biochim Biophys Acta. 1995 Oct 17;1264 (1):141-50
  • Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC. Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9 (9):1783-90
  • Wang CS, Dashti A, Jackson KW, Yeh JC, Cummings RD, Tang J. Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry. 1995 Aug 22;34 (33):10639-44
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