protein

Recombinant Human Collagen alpha-1(XI) chain

MBS718449

0.05 mg (E-Coli)

185 USD

Recombinant Protein

Recombinant Human Collagen alpha-1(XI) chain

Collagen alpha-1(XI) chain

collagen alpha-1(XI) chain isoform E preproprotein; Collagen alpha-1(XI) chain; collagen alpha-1(XI) chain; collagen type XI alpha 1

COL11A1

COL11A1; COL11A1; STL2; COLL6; CO11A1; COLL6

COBA1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

532-699

1767

GPMGLTGRPGPVGGPGSSGAKGESGDPGPQGPRGVQGPP
GPTGKPGKRGRPGADGGRGMPGEPGAKGDRGFDGLPGLP
GDKGHRGERGPQGPPGPPGDDGMRGEDGEIGPRGLPGEA
GPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGNMGPQGEP
GPPGQQGNPGPQ

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Signal Transduction

May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.

Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide and expression of the gene in tumor cell lines.Yoshioka H., Ramirez F.J. Biol. Chem. 265:6423-6426(1990) Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall syndrome, but other mutations cause overlapping Marshall/Stickler phenotypes.Annunen S., Koerkkoe J., Czarny M., Warman M.L., Brunner H.G., Kaeaeriaeinen H., Mulliken J.B., Tranebjaerg L., Brooks D.G., Cox G.F., Cruysberg J.R., Curtis M.A., Davenport S.L.H., Friedrich C.A., Kaitila I., Krawczynski M.R., Latos-Bielenska A., Mukai S., Olsen B.R., Shinno N., Somer M., Vikkula M., Zlotogora J., Prockop D.J., Ala-Kokko L.Am. J. Hum. Genet. 65:974-983(1999) 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)

299523257

NP_001177638.1

NM_001190709.1

P12107

43.2kD

Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (1270247); Collagen Biosynthesis And Modifying Enzymes Pathway (1270246); Collagen Formation Pathway (1270245); Extracellular Matrix Organization Pathway (1270244); Focal Adhesion Pathway (198795); Protein Digestion And Absorption Pathway (172847); Protein Digestion And Absorption Pathway (171868)

This gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. Mutations in this gene are associated with type II Stickler syndrome and with Marshall syndrome. A single-nucleotide polymorphism in this gene is also associated with susceptibility to lumbar disc herniation. Multiple transcript variants have been identified for this gene. [provided by RefSeq, Nov 2009]

COL11A1: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. Defects in COL11A1 are the cause of Stickler syndrome type 2 (STL2); also known as Stickler syndrome vitreous type 2. STL2 is an autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. Defects in COL11A1 are the cause of Marshall syndrome (MRSHS). It is an autosomal dominant disorder characterized by ocular abnormalities, deafness, craniofacial anomalies, and anhidrotic ectodermal dysplasia. Clinical features include short stature; flat or retruded midface with short, depressed nose, flat nasal bridge and anteverted nares; cleft palate with or without the Pierre Robin sequence; appearance of large eyes with ocular hypertelorism; cataracts, either congenital or juvenile; esotropia; high myopia; sensorineural hearing loss; spondyloepiphyseal abnormalities; calcification of the falx cerebri; ectodermal abnormalities, including defects in sweating and dental structures. Defects in COL11A1 are the cause of fibrochondrogenesis type 1 (FBCG1). A severe short-limbed skeletal dysplasia characterized by broad long-bone metaphyses, pear-shaped vertebral bodies, and characteristic morphology of the growth plate, in which the chondrocytes have a fibroblastic appearance and there are regions of fibrous cartilage extracellular matrix. Clinical features include a flat midface with a small nose and anteverted nares, significant shortening of all limb segments but relatively normal hands and feet, and a small bell-shaped thorax with a protuberant abdomen. Belongs to the fibrillar collagen family. 3 isoforms of the human protein are produced by alternative splicing. Protein type: Secreted, signal peptide; Secreted; Extracellular matrix. Chromosomal Location of Human Ortholog: 1p21. Cellular Component: collagen type XI; endoplasmic reticulum lumen; extracellular region. Molecular Function: extracellular matrix binding; extracellular matrix structural constituent; metal ion binding; protein binding, bridging. Biological Process: cartilage condensation; chondrocyte development; collagen catabolic process; collagen fibril organization; detection of mechanical stimulus involved in sensory perception of sound; embryonic skeletal morphogenesis; extracellular matrix disassembly; extracellular matrix organization and biogenesis; inner ear morphogenesis; ossification; proteoglycan metabolic process; sensory perception of sound; ventricular cardiac muscle morphogenesis; visual perception. Disease: Fibrochondrogenesis 1; Intervertebral Disc Disease; Marshall Syndrome; Stickler Syndrome, Type Ii

0.05 mg (E-Coli)

185 USD

0.2 mg (E-Coli)

420

0.5 mg (E-Coli)

680

1 mg (E-Coli)

1070