Chymotrypsin-like elastase family member 3A Recombinant Protein | CELA3A recombinant protein

Recombinant Human Chymotrypsin-like elastase family member 3A

Cat. Num. AAA968407

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Chymotrypsin-like elastase family member 3A; Recombinant Human Chymotrypsin-like elastase family member 3A; Elastase IIIA; Elastase-3A; Protease E; CELA3A recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 29-270aa; Full Length of Mature Protein
• Sequence: VVHGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISRDLTYQVVLGEYNLAVKEGPEQVIPINSEELFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNKTPCYITGWGRLYTNGPLPDKLQQARLPVVDYKHCSRWNWWGSTVKKTMVCAGGYIRSGCNGDSGGPLNCPTEDGGWQVHGVTSFVSAFGCNFIWKPTVFTRVSAFIDWIEETIASH

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for CELA3A recombinant protein

Efficient protease with alanine specificity but only little elastolytic activity.

Product Categories/Family for CELA3A recombinant protein

Cell Biology

References

Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic gene cloning.Tani T., Ohsumi J., Mita K., Takiguchi Y.J. Biol. Chem. 263:1231-1239(1988) Molecular cloning of complementary DNA encoding one of the human pancreatic protease E isozymes.Shirasu Y., Takemura K., Yoshida H., Sato Y., Iijima H., Shimada Y., Mikayama T., Ozawa T., Ikeda N., Ishida A., Tamai Y., Matsuki S., Tanaka J., Ikenaga H., Ogawa M.J. Biochem. 104:259-264(1988) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)

NCBI and Uniprot Product Information

• NCBI GI #: 236460050
• NCBI GeneID: 10136
• NCBI Accession #: NP_005738.4
• NCBI GenBank Nucleotide #: NM_005747.4
• UniProt Accession #: P09093; Q9BRW4; B1AQ53
• Molecular Weight: 42.6 kDa
• NCBI Official Full Name: chymotrypsin-like elastase family member 3A preproprotein
• UniProt Protein Name: Chymotrypsin-like elastase family member 3A
• Protein Family: Chymotrypsin-like elastase family
• UniProt Gene Name: CELA3A
• UniProt Synonym Gene Names: ELA3; ELA3A
• UniProt Entry Name: CEL3A_HUMAN

NCBI Description

Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3A has little elastolytic activity. Like most of the human elastases, elastase 3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. Elastase 3A preferentially cleaves proteins after alanine residues. Elastase 3A may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1. [provided by RefSeq, Jul 2008]

Uniprot Description

CELA3A: Efficient protease with alanine specificity but only little elastolytic activity. Belongs to the peptidase S1 family. Elastase subfamily.

Protein type: Protease; EC 3.4.21.70

Chromosomal Location of Human Ortholog: 1p36.12

Cellular Component: extracellular space

Molecular Function: serine-type endopeptidase activity

Biological Process: cholesterol metabolic process; digestion; proteolysis