COL1A1 sirna

COL1A1 siRNA (Rat)

Cat. Num. AAA8239931

• Gene Names: Col1a1; COLIA1
• Reactivity: Rat
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: COL1A1; COL1A1 siRNA (Rat); Collagen alpha-1(I) chain; Alpha-1 type I collagen; COL1A1 sirna

• Host: Synthetic
• Reactivity: Rat
• Specificity: COL1A1 siRNA (Rat) is a target-specific 19-23 nt siRNA oligo duplexes designed to knock down gene expression.
• Purity/Purification: > 97%
• Form/Format: Lyophilized powder
• Sequence Length: 1453

• Applicable Applications for COL1A1 sirna: RNA Interference (RNAi)
• Quality Control: Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
• Directions for Use: We recommends transfection with 100 nM siRNA 48 to 72 hours prior to cell lysis. Before resuspending, briefly centrifuge the tube to ensure the lyophilized siRNA is at the bottom of the tube. Resuspend the siRNA oligos to an appropriate concentration with DEPC water. For each vial, suitable for 250 transfections in 24 well plate (20 pmol for each well).
• Components: We offer pre-designed sets of 3 different target-specific siRNA oligo duplexes of rat COL1A1 gene. Each vial contains 5 nmol of lyophilized siRNA. The duplexes can be transfected individually or pooled together to achieve knockdown of the target gene, which is most commonly assessed by qPCR or western blot. Our siRNA oligos are also chemically modified (2'-OMe) at no extra charge for increased stability and enhanced knockdown in vitro and in vivo.
• Preparation and Storage: Shipped at 4 degree C. Store at -20 degree C for one year.

Related Product Information for COL1A1 sirna

siRNA to inhibit COL1A1 expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 158711704
• NCBI GeneID: 29393
• NCBI Accession #: NP_445756.1
• NCBI GenBank Nucleotide #: NM_053304.1
• UniProt Accession #: P02454; P02455; Q63079; A3KNA1
• Molecular Weight: 137,953 Da
• NCBI Official Full Name: collagen alpha-1(I) chain
• NCBI Official Synonym Full Names: collagen, type I, alpha 1
• NCBI Official Symbol: Col1a1
• NCBI Official Synonym Symbols: COLIA1
• NCBI Protein Information: collagen alpha-1(I) chain
• UniProt Protein Name: Collagen alpha-1(I) chain
• Protein Family: Collagen
• UniProt Gene Name: Col1a1
• UniProt Entry Name: CO1A1_RAT

NCBI Description

extracellular matrix collagen protein [RGD, Feb 2006]

Uniprot Description

COL1A1: Type I collagen is a member of group I collagen (fibrillar forming collagen). Defects in COL1A1 are the cause of Caffey disease (CAFFD); also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1); also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome. Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A); also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1). A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2); also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3). A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4); also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP); also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture. A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF. Belongs to the fibrillar collagen family.

Protein type: Secreted, signal peptide; Secreted; Extracellular matrix

Cellular Component: extracellular matrix; Golgi apparatus; proteinaceous extracellular matrix; extracellular space; collagen; endoplasmic reticulum; cytoplasm; extracellular region; collagen type I; secretory granule

Molecular Function: identical protein binding; protein binding; metal ion binding; platelet-derived growth factor binding; extracellular matrix structural constituent

Biological Process: skin development; response to peptide hormone stimulus; intramembranous ossification; response to cAMP; collagen fibril organization; wound healing; embryonic skeletal development; positive regulation of transcription, DNA-dependent; response to estradiol stimulus; response to corticosteroid stimulus; protein transport; sensory perception of sound; visual perception; skeletal development; collagen biosynthetic process; response to nutrient; endochondral ossification; response to nutrient levels; response to drug; blood vessel development; ossification; skin morphogenesis; osteoblast differentiation; response to hyperoxia; response to hydrogen peroxide; response to steroid hormone stimulus; skeletal morphogenesis; response to mechanical stimulus; positive regulation of cell migration